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Conserved domains on  [gi|1570466244|ref|XP_027967058|]
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diacylglycerol kinase zeta isoform X2 [Eumetopias jubatus]

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 ...
 829-986 1.38e-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: 249.94  E-value: 1.38e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   829 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGTDLTPKIqdlKPQCI 908
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   909 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVVLT--TSKAIPVQVD 983
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                    ...
gi 1570466244   984 GEP 986
Cdd:smart00045  158 GEP 160
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 680-801 1.26e-51

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: 177.49  E-value: 1.26e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   680 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 757
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1570466244   758 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 801
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 553-627 4.01e-51

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: 174.12  E-value: 4.01e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570466244  553 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTW 627
Cdd:cd20895      1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 401-543 9.22e-41

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 cd20849:

Pssm-ID: 412127  Cd Length: 74  Bit Score: 144.31  E-value: 9.22e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  401 DWSESATYGEHIWFETNVSGDFCYVGEQYCVAKMLQKSVSRRKCAACKIVVHTPCIEQLEKpltpragfphscaeaeagt 480
Cdd:cd20849      1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEK------------------- 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1570466244  481 vgkretnlapgvpepevetkpvstdelmvsrdrpaqvcqqgsgrlhvprrINFRCKPSFRESG 543
Cdd:cd20849     62 --------------------------------------------------INFRCKPSFRESG 74
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1322 1.93e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.93e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1206 LIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 1284
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDN---DGNTPLHLAAANGNLE 167

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1570466244 1285 ICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYL 1322
Cdd:COG0666    168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 100-388 4.46e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.86  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  100 WRAGAPPPWADLLQAHRnleGCWAHPPGPAmetfFRRRFQWKAPGPGEGQRRPSGVGLPTGKARRRSPAGQASSSLVQRR 179
Cdd:COG3321    841 WVAGVPVDWSALYPGRG---RRRVPLPTYP----FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAA 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  180 RSSAQLQGCLLSCGVGARGTSRRRSSTVPPACSPRFVVDEVLAPQPAAVGAQPLGTPLLLAEIIGVPEEDVAAAALRATQ 259
Cdd:COG3321    914 AAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAA 993

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  260 PGAKRPGSSSHRGTLVPMLRCLRRHRPSTPLLPADVVYDHALWGLHGYYRRLSQQRPPGQHPGPGARRASGTAAGALMPT 339
Cdd:COG3321    994 AALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAA 1073

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1570466244  340 RVRPLSRRRQVALRRKSAGPQTWSALLAKAITKSGLQHLAPPPPTPGAL 388
Cdd:COG3321   1074 LAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAA 1122
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 829-986 1.38e-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: 249.94  E-value: 1.38e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   829 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGTDLTPKIqdlKPQCI 908
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   909 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVVLT--TSKAIPVQVD 983
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                    ...
gi 1570466244   984 GEP 986
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 829-986 1.74e-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: 227.10  E-value: 1.74e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  829 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGTDLTPKiqdLKPQCI 908
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  909 VFLNIPRYCAGTMPWGHPGEHHD-FEPQRHDDGYLEVIGFT-MTSLAALQVGGHGE-RLTQCREVVLTTSKAIPVQVDGE 985
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1570466244  986 P 986
Cdd:pfam00609  158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 680-801 1.26e-51

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: 177.49  E-value: 1.26e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   680 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 757
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1570466244   758 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 801
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 553-627 4.01e-51

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: 174.12  E-value: 4.01e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570466244  553 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTW 627
Cdd:cd20895      1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 401-543 9.22e-41

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: 144.31  E-value: 9.22e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  401 DWSESATYGEHIWFETNVSGDFCYVGEQYCVAKMLQKSVSRRKCAACKIVVHTPCIEQLEKpltpragfphscaeaeagt 480
Cdd:cd20849      1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEK------------------- 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1570466244  481 vgkretnlapgvpepevetkpvstdelmvsrdrpaqvcqqgsgrlhvprrINFRCKPSFRESG 543
Cdd:cd20849     62 --------------------------------------------------INFRCKPSFRESG 74
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 678-800 2.63e-35

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: 130.78  E-value: 2.63e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  678 PLLVFVNPKSGGNQGAKIIQSFLWYLNPRQV-FDLSQ-GGPKEALEMYRKV---HNLRILACGGDGTVGWILSTLDqlRL 752
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAaedGYDRIVVAGGDGTVNEVLNGLA--GL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1570466244  753 KPPPPVAILPLGTGNDLARTLNWGGgytdePVSKILSHVEEGNVVQLD 800
Cdd:pfam00781   79 ATRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 676-999 2.10e-26

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 110.71  E-value: 2.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  676 MKPLLVFVNPKSGGNQGAKIIQSFLWYLNpRQVFDLSQ---GGPKEALEMYRKVHNL---RILACGGDGTVGWILSTLdq 749
Cdd:COG1597      2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  750 lrLKPPPPVAILPLGTGNDLARTLNwgggyTDEPVSKILSHVEEGNVVQLD--RwdlraepnpdagpeerddgATDRLpl 827
Cdd:COG1597     79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDlgR-------------------VNGRY-- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  828 dvFNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlAKHIRVVCDGTDLTpkiqdLKPQC 907
Cdd:COG1597    131 --FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDGEEIE-----GEALL 191

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  908 IVFLNIPRYcagtmpwghpGEHHDFEPQ-RHDDGYLEVIGFT-------MTSLAALQVGGHGE----RLTQCREVVLTTS 975
Cdd:COG1597    192 VAVGNGPYY----------GGGLRLAPDaSLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESD 261

                          330       340
                   ....*....|....*....|....*...
gi 1570466244  976 KAIPVQVDGEPCKLAAS-RIRI---ALR 999
Cdd:COG1597    262 RPLPVQLDGEPLGLATPlEFEVlpgALR 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1322 1.93e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.93e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1206 LIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 1284
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDN---DGNTPLHLAAANGNLE 167

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1570466244 1285 ICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYL 1322
Cdd:COG0666    168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1206-1300 3.80e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 3.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1206 LIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDaveeNGETCLHQAAALGQRTI 1285
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 1570466244 1286 CHYIVEAGASLMKTD 1300
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PRK12361 PRK12361
hypothetical protein; Provisional
 677-800 3.34e-08

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 57.71  E-value: 3.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  677 KPLLVFVNPKSGGNQGAKIIQSFLWYLNPRqvFDLS--QGGP--------KEALEmyRKVHnlRILACGGDGTVGWILST 746
Cdd:PRK12361   243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPeisaealaKQARK--AGAD--IVIACGGDGTVTEVASE 316

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1570466244  747 L--DQLRLkppppvAILPLGTGNDLARTLnWGGGYTDEPVSKILSHVEEGNVVQLD 800
Cdd:PRK12361   317 LvnTDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQGHTQRID 365
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 555-614 9.04e-08

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 49.75  E-value: 9.04e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570466244  555 HHWVHRR-RQDGKCRHCGKgfqqkfTFHSKEIVAISCSWCKQAYHSKvsCFMLQQIEEPCS 614
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1212-1306 1.29e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1212 RNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSK---DVVRYLLDHAppeILDAVEENGETCLHQAAALGQRTICHY 1288
Cdd:PHA03095   199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrsLVLPLLIAGI---SINARNRYGQTPLHYAAVFNNPRACRR 275

                           90
                   ....*....|....*...
gi 1570466244 1289 IVEAGASLMKTDQQGDTP 1306
Cdd:PHA03095   276 LIALGADINAVSSDGNTP 293
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 100-388 4.46e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.86  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  100 WRAGAPPPWADLLQAHRnleGCWAHPPGPAmetfFRRRFQWKAPGPGEGQRRPSGVGLPTGKARRRSPAGQASSSLVQRR 179
Cdd:COG3321    841 WVAGVPVDWSALYPGRG---RRRVPLPTYP----FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAA 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  180 RSSAQLQGCLLSCGVGARGTSRRRSSTVPPACSPRFVVDEVLAPQPAAVGAQPLGTPLLLAEIIGVPEEDVAAAALRATQ 259
Cdd:COG3321    914 AAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAA 993

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  260 PGAKRPGSSSHRGTLVPMLRCLRRHRPSTPLLPADVVYDHALWGLHGYYRRLSQQRPPGQHPGPGARRASGTAAGALMPT 339
Cdd:COG3321    994 AALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAA 1073

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1570466244  340 RVRPLSRRRQVALRRKSAGPQTWSALLAKAITKSGLQHLAPPPPTPGAL 388
Cdd:COG3321   1074 LAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAA 1122
PHA03247 PHA03247
large tegument protein UL36; Provisional
 22-394 1.72e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   22 PAEALGTEEGERPGALRQMWRYRSWDVPQIPAEAPRTQAWRQNHWETSSEGPMHPRGTVS----GPLGFHCPPPGPPGTS 97
Cdd:PHA03247  2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAArptvGSLTSLADPPPPPPTP 2708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   98 ASwragAPPPWADLLQAhrnlegcwahPPGPAMEtffrRRFQWKAPGPGEGQRRPSGVGLPTGKARRRSPAGQASSslvq 177
Cdd:PHA03247  2709 EP----APHALVSATPL----------PPGPAAA----RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP---- 2766

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  178 rrrssaqlqgcllscgvgARGTSRRRSSTVPPACSPRfvvdevLAPQPAAVGAQPLGTPlllaeiigvpeEDVAAAALRA 257
Cdd:PHA03247  2767 ------------------PAPAPPAAPAAGPPRRLTR------PAVASLSESRESLPSP-----------WDPADPPAAV 2811

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  258 TQPGAKRPGSSSHRGTLVPMLRCLRRHRPSTPLLPADvvydhalwglhgyYRRLSQQRPPGqhpGPGARRASGTAAGALM 337
Cdd:PHA03247  2812 LAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP-------------SLPLGGSVAPG---GDVRRRPPSRSPAAKP 2875

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1570466244  338 PTRVRPLSRRrqvaLRRKSAGPQTWSALLAKAITKSGLQHLAPPPPTPGALCSEPER 394
Cdd:PHA03247  2876 AAPARPPVRR----LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 730-773 2.71e-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: 41.34  E-value: 2.71e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1570466244  730 RILACGGDGTVGWILSTLDQLRLKPPppVAILPLGTGNDLARTL 773
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNALIQLDDIPA--LGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1236-1257 3.21e-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: 36.41  E-value: 3.21e-03
                            10        20
                    ....*....|....*....|..
gi 1570466244  1236 RTLLHHAVSTGSKDVVRYLLDH 1257
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDK 24
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 829-986 1.38e-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: 249.94  E-value: 1.38e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   829 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGTDLTPKIqdlKPQCI 908
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   909 VFLNIPRYCAGTMPWGHPGEH-HDFEPQRHDDGYLEVIGFTMTSLAA--LQVGGHGERLTQCREVVLT--TSKAIPVQVD 983
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEdLNFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVRITikTSKTIPMQVD 157


                    ...
gi 1570466244   984 GEP 986
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 829-986 1.74e-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: 227.10  E-value: 1.74e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  829 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGTDLTPKiqdLKPQCI 908
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  909 VFLNIPRYCAGTMPWGHPGEHHD-FEPQRHDDGYLEVIGFT-MTSLAALQVGGHGE-RLTQCREVVLTTSKAIPVQVDGE 985
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1570466244  986 P 986
Cdd:pfam00609  158 P 158
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 680-801 1.26e-51

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: 177.49  E-value: 1.26e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   680 LVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHN-LRILACGGDGTVGWILSTLDQLRLKPP-PP 757
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1570466244   758 VAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDR 801
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 553-627 4.01e-51

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: 174.12  E-value: 4.01e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570466244  553 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTW 627
Cdd:cd20895      1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 553-627 6.27e-46

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: 159.48  E-value: 6.27e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570466244  553 VRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTW 627
Cdd:cd20896      1 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 555-616 3.21e-42

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: 148.26  E-value: 3.21e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1570466244  555 HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLG 616
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKSFQQKLSFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 401-543 9.22e-41

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: 144.31  E-value: 9.22e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  401 DWSESATYGEHIWFETNVSGDFCYVGEQYCVAKMLQKSVSRRKCAACKIVVHTPCIEQLEKpltpragfphscaeaeagt 480
Cdd:cd20849      1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKQLQKSVSRKKCAACKIVVHTPCIEQLEK------------------- 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1570466244  481 vgkretnlapgvpepevetkpvstdelmvsrdrpaqvcqqgsgrlhvprrINFRCKPSFRESG 543
Cdd:cd20849     62 --------------------------------------------------INFRCKPSFRESG 74
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 678-800 2.63e-35

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: 130.78  E-value: 2.63e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  678 PLLVFVNPKSGGNQGAKIIQSFLWYLNPRQV-FDLSQ-GGPKEALEMYRKV---HNLRILACGGDGTVGWILSTLDqlRL 752
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAaedGYDRIVVAGGDGTVNEVLNGLA--GL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1570466244  753 KPPPPVAILPLGTGNDLARTLNWGGgytdePVSKILSHVEEGNVVQLD 800
Cdd:pfam00781   79 ATRPPLGIIPLGTGNDFARALGIPG-----DPEEALEAILKGQTRPVD 121
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 401-461 6.67e-28

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: 107.80  E-value: 6.67e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570466244  401 DWSESATYGEHIWFETNVSGDFCYVGEQYCVAKmLQKSVSRRKCAACKIVVHTPCIEQLEK 461
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVK-FAKSALRRKCAACKIVVHTACIEQLEK 60
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 676-999 2.10e-26

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 110.71  E-value: 2.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  676 MKPLLVFVNPKSGGNQGAKIIQSFLWYLNpRQVFDLSQ---GGPKEALEMYRKVHNL---RILACGGDGTVGWILSTLdq 749
Cdd:COG1597      2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  750 lrLKPPPPVAILPLGTGNDLARTLNwgggyTDEPVSKILSHVEEGNVVQLD--RwdlraepnpdagpeerddgATDRLpl 827
Cdd:COG1597     79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDlgR-------------------VNGRY-- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  828 dvFNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGTAFSdfLMGSSKdlAKHIRVVCDGTDLTpkiqdLKPQC 907
Cdd:COG1597    131 --FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALR--ALLRYR--PFRLRIELDGEEIE-----GEALL 191

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  908 IVFLNIPRYcagtmpwghpGEHHDFEPQ-RHDDGYLEVIGFT-------MTSLAALQVGGHGE----RLTQCREVVLTTS 975
Cdd:COG1597    192 VAVGNGPYY----------GGGLRLAPDaSLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIESD 261

                          330       340
                   ....*....|....*....|....*...
gi 1570466244  976 KAIPVQVDGEPCKLAAS-RIRI---ALR 999
Cdd:COG1597    262 RPLPVQLDGEPLGLATPlEFEVlpgALR 289
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 406-461 3.27e-26

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: 102.37  E-value: 3.27e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1570466244  406 ATYGEHIWFETNVSGDFCYVGEQYCvakmlQKSVSRRKCAACKIVVHTPCIEQLEK 461
Cdd:cd20802      1 AVNGEHLWTDTSASGDLCYVGEQDC-----LKSGSRKKCSACKIVVHTGCIPQLEK 51
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1322 1.93e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.93e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1206 LIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 1284
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDN---DGNTPLHLAAANGNLE 167

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1570466244 1285 ICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYL 1322
Cdd:COG0666    168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1206-1300 3.80e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 3.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1206 LIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDaveeNGETCLHQAAALGQRTI 1285
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 1570466244 1286 CHYIVEAGASLMKTD 1300
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1339 1.92e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 1.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1206 LIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDAveeNGETCLHQAAALGQRT 1284
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAgADVNAKDN---DGKTALDLAAENGNLE 233

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1570466244 1285 ICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETA 1339
Cdd:COG0666    234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 555-616 3.87e-12

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: 62.46  E-value: 3.87e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1570466244  555 HHWVHRRRQ-DGKCRHCGKGFQQKFTFHSKeivaiSCSWCKQAYHSkvSCFMLQQIEEpCSLG 616
Cdd:cd20805      1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY-----RCSWCKRTVHS--ECIDKLGPEE-CDLG 55
PRK12361 PRK12361
hypothetical protein; Provisional
 677-800 3.34e-08

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 57.71  E-value: 3.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  677 KPLLVFVNPKSGGNQGAKIIQSFLWYLNPRqvFDLS--QGGP--------KEALEmyRKVHnlRILACGGDGTVGWILST 746
Cdd:PRK12361   243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvkLTTPeisaealaKQARK--AGAD--IVIACGGDGTVTEVASE 316

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1570466244  747 L--DQLRLkppppvAILPLGTGNDLARTLnWGGGYTDEPVSKILSHVEEGNVVQLD 800
Cdd:PRK12361   317 LvnTDITL------GIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQGHTQRID 365
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 555-614 9.04e-08

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 49.75  E-value: 9.04e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570466244  555 HHWVHRR-RQDGKCRHCGKgfqqkfTFHSKEIVAISCSWCKQAYHSKvsCFMLQQIEEPCS 614
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
1236-1290 1.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1570466244 1236 RTLLHHAVSTGSKDVVRYLLDHAPPeiLDAVEENGETCLHQAAALGQRTICHYIV 1290
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD--INAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1206-1322 2.56e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.72  E-value: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1206 LIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPeiLDAVEENGETCLHQAAALGQRTI 1285
Cdd:COG0666     25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD--INAKDDGGNTLLHAAARNGDLEI 102

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1570466244 1286 CHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYL 1322
Cdd:COG0666    103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PRK13054 PRK13054
lipid kinase; Reviewed
 730-771 2.60e-06

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 51.03  E-value: 2.60e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1570466244  730 RILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLAR 771
Cdd:PRK13054    59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
PRK13059 PRK13059
putative lipid kinase; Reviewed
 676-774 7.51e-06

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 49.26  E-value: 7.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  676 MKPLLVFVNPKSGGNQGA----KIIQSFLWYLNPRQVFDLSQGGP-KEALEMYRKVHNLrILACGGDGTVGWILSTLDQL 750
Cdd:PRK13059     1 MKKVKFIYNPYSGENAIIseldKVIRIHQEKGYLVVPYRISLEYDlKNAFKDIDESYKY-ILIAGGDGTVDNVVNAMKKL 79

                           90       100
                   ....*....|....*....|....
gi 1570466244  751 RLKPPppVAILPLGTGNDLARTLN 774
Cdd:PRK13059    80 NIDLP--IGILPVGTANDFAKFLG 101
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1239-1322 1.16e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1239 LHHAVSTGSKDVVRYLLDHapPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDqqGDTPRQRAEKAQDTEL 1318
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN--GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEI 76


                   ....
gi 1570466244 1319 AAYL 1322
Cdd:pfam12796   77 VKLL 80
PRK13055 PRK13055
putative lipid kinase; Reviewed
 731-774 4.15e-05

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 47.29  E-value: 4.15e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1570466244  731 ILACGGDGTVGWILSTLDQlrLKPPPPVAILPLGTGNDLARTLN 774
Cdd:PRK13055    63 IIAAGGDGTINEVVNGIAP--LEKRPKMAIIPAGTTNDYARALK 104
Ank_4 pfam13637
Ankyrin repeats (many copies);
1206-1255 4.89e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.89e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1206 LIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLL 1255
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PRK13057 PRK13057
lipid kinase;
718-774 5.44e-05

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 46.83  E-value: 5.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1570466244  718 EALEMYRKVHNLRILAcGGDGTVGWILSTLDQLRLkpppPVAILPLGTGNDLARTLN 774
Cdd:PRK13057    42 EVIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL----PLGILPLGTANDLARTLG 93
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1212-1306 1.29e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1212 RNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSK---DVVRYLLDHAppeILDAVEENGETCLHQAAALGQRTICHY 1288
Cdd:PHA03095   199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrsLVLPLLIAGI---SINARNRYGQTPLHYAAVFNNPRACRR 275

                           90
                   ....*....|....*...
gi 1570466244 1289 IVEAGASLMKTDQQGDTP 1306
Cdd:PHA03095   276 LIALGADINAVSSDGNTP 293
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 100-388 4.46e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.86  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  100 WRAGAPPPWADLLQAHRnleGCWAHPPGPAmetfFRRRFQWKAPGPGEGQRRPSGVGLPTGKARRRSPAGQASSSLVQRR 179
Cdd:COG3321    841 WVAGVPVDWSALYPGRG---RRRVPLPTYP----FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAA 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  180 RSSAQLQGCLLSCGVGARGTSRRRSSTVPPACSPRFVVDEVLAPQPAAVGAQPLGTPLLLAEIIGVPEEDVAAAALRATQ 259
Cdd:COG3321    914 AAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAA 993

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  260 PGAKRPGSSSHRGTLVPMLRCLRRHRPSTPLLPADVVYDHALWGLHGYYRRLSQQRPPGQHPGPGARRASGTAAGALMPT 339
Cdd:COG3321    994 AALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAA 1073

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1570466244  340 RVRPLSRRRQVALRRKSAGPQTWSALLAKAITKSGLQHLAPPPPTPGAL 388
Cdd:COG3321   1074 LAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAA 1122
Ank_5 pfam13857
Ankyrin repeats (many copies);
1221-1277 1.53e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1570466244 1221 LHRAGG-DLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHapPEILDAVEENGETCLHQA 1277
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEEGLTALDLA 56
PHA03247 PHA03247
large tegument protein UL36; Provisional
 22-394 1.72e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   22 PAEALGTEEGERPGALRQMWRYRSWDVPQIPAEAPRTQAWRQNHWETSSEGPMHPRGTVS----GPLGFHCPPPGPPGTS 97
Cdd:PHA03247  2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAArptvGSLTSLADPPPPPPTP 2708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   98 ASwragAPPPWADLLQAhrnlegcwahPPGPAMEtffrRRFQWKAPGPGEGQRRPSGVGLPTGKARRRSPAGQASSslvq 177
Cdd:PHA03247  2709 EP----APHALVSATPL----------PPGPAAA----RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP---- 2766

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  178 rrrssaqlqgcllscgvgARGTSRRRSSTVPPACSPRfvvdevLAPQPAAVGAQPLGTPlllaeiigvpeEDVAAAALRA 257
Cdd:PHA03247  2767 ------------------PAPAPPAAPAAGPPRRLTR------PAVASLSESRESLPSP-----------WDPADPPAAV 2811

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  258 TQPGAKRPGSSSHRGTLVPMLRCLRRHRPSTPLLPADvvydhalwglhgyYRRLSQQRPPGqhpGPGARRASGTAAGALM 337
Cdd:PHA03247  2812 LAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP-------------SLPLGGSVAPG---GDVRRRPPSRSPAAKP 2875

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1570466244  338 PTRVRPLSRRrqvaLRRKSAGPQTWSALLAKAITKSGLQHLAPPPPTPGALCSEPER 394
Cdd:PHA03247  2876 AAPARPPVRR----LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1197-1285 2.26e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1197 DAAPPKGEELIEAAKRNNFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHA-PPEILDAveeNGETCLH 1275
Cdd:PLN03192   520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAcNVHIRDA---NGNTALW 596

                           90
                   ....*....|
gi 1570466244 1276 QAAALGQRTI 1285
Cdd:PLN03192   597 NAISAKHHKI 606
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 730-773 2.71e-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: 41.34  E-value: 2.71e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1570466244  730 RILACGGDGTVGWILSTLDQLRLKPPppVAILPLGTGNDLARTL 773
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNALIQLDDIPA--LGILPLGTANDFARSL 101
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1236-1257 3.21e-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: 36.41  E-value: 3.21e-03
                            10        20
                    ....*....|....*....|..
gi 1570466244  1236 RTLLHHAVSTGSKDVVRYLLDH 1257
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDK 24
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1224-1322 6.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1224 AGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDaveENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQ 1302
Cdd:PHA02874   113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYgADVNIED---DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                           90       100
                   ....*....|....*....|
gi 1570466244 1303 GDTPRQRAEKAQDTELAAYL 1322
Cdd:PHA02874   190 GESPLHNAAEYGDYACIKLL 209
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 89-262 7.73e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244   89 PPPGPPGTSASWRAGAPPPWADLLQAHRNLEGCWAHPPGPAMETFFRRRFQWKAPGPGEGQrrPSGVGLPTGKARRRSPA 168
Cdd:PRK07764   617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA--PAAPPPAPAPAAPAAPA 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570466244  169 GQASSSLVQRRR---SSAQLQGCLLSCGVGARGTSRRRSSTVPPACSPRFVVDEVLAPQPAAVGAQPLgtplllaeiiGV 245
Cdd:PRK07764   695 GAAPAQPAPAPAatpPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPP----------AP 764

                          170
                   ....*....|....*..
gi 1570466244  246 PEEDVAAAALRATQPGA 262
Cdd:PRK07764   765 APAAAPAAAPPPSPPSE 781
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1231-1279 8.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 8.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1570466244 1231 RDEQSRTLLHHAVSTGSKDVVRYLLDH-APPEILDaveENGETCLHQAAA 1279
Cdd:PHA03100   188 KDVYGFTPLHYAVYNNNPEFVKYLLDLgANPNLVN---KYGDTPLHIAIL 234
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 411-462 9.18e-03

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.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 35.57  E-value: 9.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1570466244  411 HIWFETNV-SGDFCYVgeqyCVAKMLQKSVSRRKCAACKIVVHTPCIEQLEKP 462
Cdd:cd00029      1 HRFVPTTFsSPTFCDV----CGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSP 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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