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Conserved domains on  [gi|1663473103|ref|XP_029141388|]
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diacylglycerol kinase iota [Protobothrops mucrosquamatus]

Protein Classification

diacylglycerol kinase( domain architecture ID 19123894)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 510-667 2.88e-73

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: 239.16  E-value: 2.88e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   510 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTSKIqelKFQCI 589
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   590 VFLNIPRYCAGTMPWGNPGDHRE-FEPQRHDDGFIEVIGFTMASLAA--LQVGGHGERLHQCREV--TLLTYKSIPMQVD 664
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEDLnFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1663473103   665 GEP 667
Cdd:smart00045  158 GEP 160
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 234-308 3.49e-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: 3.49e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663473103  234 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFLLQHIEEPCSLGAHAAVIIPPTW 308
Cdd:cd20895      1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 153-225 5.67e-49

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: 167.51  E-value: 5.67e-49
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1663473103  153 EWSENAINGEHLWLETNVSGDLCYLGEEGCQVKFSKSAVRRKCAACKIVVHNACMEQLEKINFRCKPTFREGS 225
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 362-483 2.70e-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: 161.70  E-value: 2.70e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   362 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPRDALELYRKMPN-LRILACGGDGTVGWILSILDELQLNPQ-PP 439
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1663473103   440 VAVLPLGTGNDLARTLNWGGGYTDEPVAKILCHVEDGAIVQLDR 483
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
924-1041 2.83e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 2.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  924 KKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSelLDMTDSEtGETALHKAACQRHRGICQMLVEAGASLGKMDS 1003
Cdd:COG0666    141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1663473103 1004 KGKTPRDRAQQAGDPDLASYLESHQNYPVVPHEDLETA 1041
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 510-667 2.88e-73

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: 239.16  E-value: 2.88e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   510 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTSKIqelKFQCI 589
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   590 VFLNIPRYCAGTMPWGNPGDHRE-FEPQRHDDGFIEVIGFTMASLAA--LQVGGHGERLHQCREV--TLLTYKSIPMQVD 664
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEDLnFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1663473103   665 GEP 667
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 510-667 1.14e-66

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: 220.94  E-value: 1.14e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  510 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTSKiqeLKFQCI 589
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  590 VFLNIPRYCAGTMPWGNPGDHRE-FEPQRHDDGFIEVIGFT-MASLAALQVGGHGE-RLHQCREVTLLTYKSIPMQVDGE 666
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1663473103  667 P 667
Cdd:pfam00609  158 P 158
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 234-308 3.49e-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: 3.49e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663473103  234 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFLLQHIEEPCSLGAHAAVIIPPTW 308
Cdd:cd20895      1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 153-225 5.67e-49

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: 167.51  E-value: 5.67e-49
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1663473103  153 EWSENAINGEHLWLETNVSGDLCYLGEEGCQVKFSKSAVRRKCAACKIVVHNACMEQLEKINFRCKPTFREGS 225
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 362-483 2.70e-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: 161.70  E-value: 2.70e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   362 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPRDALELYRKMPN-LRILACGGDGTVGWILSILDELQLNPQ-PP 439
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1663473103   440 VAVLPLGTGNDLARTLNWGGGYTDEPVAKILCHVEDGAIVQLDR 483
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 360-459 2.97e-33

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: 124.62  E-value: 2.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  360 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPRDALELYRKMPNL---RILACGGDGTVGWILSILDELQl 434
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLA- 79

                           90       100
                   ....*....|....*....|....*
gi 1663473103  435 nPQPPVAVLPLGTGNDLARTLNWGG 459
Cdd:pfam00781   80 -TRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 358-683 3.08e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 113.02  E-value: 3.08e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  358 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPRDALELYRKMPNL---RILACGGDGTVGWILSILde 431
Cdd:COG1597      2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  432 lqLNPQPPVAVLPLGTGNDLARTLNwgggyTDEPVAKILCHVEDGAIVQLD------RWnlqvernpdlppkeledgtqk 505
Cdd:COG1597     79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDlgrvngRY--------------------- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  506 lplnvFNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLtskiqELK 585
Cdd:COG1597    131 -----FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEI-----EGE 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  586 FQCIVFLNIPRYcaGTMPWGNPGDhrefepqRHDDGFIEVIGFT-------MASLAALQVGGHGE----RLHQCREVTLL 654
Cdd:COG1597    189 ALLVAVGNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIE 259

                          330       340
                   ....*....|....*....|....*....
gi 1663473103  655 TYKSIPMQVDGEPCRLAPSlIRISLRNQA 683
Cdd:COG1597    260 SDRPLPVQLDGEPLGLATP-LEFEVLPGA 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
924-1041 2.83e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 2.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  924 KKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSelLDMTDSEtGETALHKAACQRHRGICQMLVEAGASLGKMDS 1003
Cdd:COG0666    141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1663473103 1004 KGKTPRDRAQQAGDPDLASYLESHQNYPVVPHEDLETA 1041
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
907-1002 7.60e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 7.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  907 LLQSVIAGDfLRFVEW-CKKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSELLDMtdsetGETALHKAACQRHR 985
Cdd:pfam12796    1 LHLAAKNGN-LELVKLlLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1663473103  986 GICQMLVEAGASLGKMD 1002
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 236-295 1.12e-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: 52.06  E-value: 1.12e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663473103  236 HHWVHRR-RQEGKCKQCGKgfqqkfSFHSKEIVAISCSWCKQAFHNKvtCFLLQHIEEPCS 295
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13057 PRK13057
lipid kinase;
362-456 2.42e-07

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 53.38  E-value: 2.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  362 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGP------RDALELYRKMPNLRILAcGGDGTVGWILSILDELQLn 435
Cdd:PRK13057     1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAedpddlSEVIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                           90       100
                   ....*....|....*....|.
gi 1663473103  436 pqpPVAVLPLGTGNDLARTLN 456
Cdd:PRK13057    76 ---PLGILPLGTANDLARTLG 93
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 926-1030 2.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  926 GANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSelLDMTDsETGETALHKAACQRHRGICQMLVEAGASLGKMDSKG 1005
Cdd:PHA02874   114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD--VNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                           90       100
                   ....*....|....*....|....*
gi 1663473103 1006 KTPRDRAQQAGDPDLASYLESHQNY 1030
Cdd:PHA02874   191 ESPLHNAAEYGDYACIKLLIDHGNH 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 935-961 3.78e-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: 3.78e-03
                            10        20
                    ....*....|....*....|....*..
gi 1663473103   935 DHCSLLHHAAKTGHGEIVKYILEHGSS 961
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 412-455 4.84e-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: 40.18  E-value: 4.84e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1663473103  412 RILACGGDGTVGWILSILdeLQLNPQPPVAVLPLGTGNDLARTL 455
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 510-667 2.88e-73

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: 239.16  E-value: 2.88e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   510 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTSKIqelKFQCI 589
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPN---SLEGI 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   590 VFLNIPRYCAGTMPWGNPGDHRE-FEPQRHDDGFIEVIGFTMASLAA--LQVGGHGERLHQCREV--TLLTYKSIPMQVD 664
Cdd:smart00045   78 AVLNIPSYGGGTNLWGTTDKEDLnFSKQSHDDGLLEVVGLTGAMHMAqiRQVGLAGRRIAQCSEVriTIKTSKTIPMQVD 157


                    ...
gi 1663473103   665 GEP 667
Cdd:smart00045  158 GEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 510-667 1.14e-66

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: 220.94  E-value: 1.14e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  510 VFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTSKiqeLKFQCI 589
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLP---KSLEGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  590 VFLNIPRYCAGTMPWGNPGDHRE-FEPQRHDDGFIEVIGFT-MASLAALQVGGHGE-RLHQCREVTLLTYKSIPMQVDGE 666
Cdd:pfam00609   78 VVLNIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTgALHLGQVQVGLGSAkRIAQGGPIRITTKKKIPMQVDGE 157


                   .
gi 1663473103  667 P 667
Cdd:pfam00609  158 P 158
C1_DGKzeta_rpt2 cd20895
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta ...
 234-308 3.49e-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: 3.49e-51
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663473103  234 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFLLQHIEEPCSLGAHAAVIIPPTW 308
Cdd:cd20895      1 VRHHWVHRRRQEGKCRQCGKGFQQKFAFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt2 cd20896
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota ...
 234-308 1.63e-50

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: 172.20  E-value: 1.63e-50
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663473103  234 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFLLQHIEEPCSLGAHAAVIIPPTW 308
Cdd:cd20896      1 VRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTW 75
C1_DGKiota_rpt1 cd20850
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase iota (DAG ...
 153-225 5.67e-49

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: 167.51  E-value: 5.67e-49
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1663473103  153 EWSENAINGEHLWLETNVSGDLCYLGEEGCQVKFSKSAVRRKCAACKIVVHNACMEQLEKINFRCKPTFREGS 225
Cdd:cd20850      1 DWSENAVNGEHLWLETNVSGDLCYLGEENCQVKFAKSALRRKCAACKIVVHTACIEQLEKINFRCKPTFREGG 73
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 362-483 2.70e-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: 161.70  E-value: 2.70e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103   362 LVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPRDALELYRKMPN-LRILACGGDGTVGWILSILDELQLNPQ-PP 439
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDfNRVLVCGGDGTVGWVLNALDKRELPLPePP 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1663473103   440 VAVLPLGTGNDLARTLNWGGGYTDEPVAKILCHVEDGAIVQLDR 483
Cdd:smart00046   81 VAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESDTVKLDR 124
C1_DGK_typeIV_rpt2 cd20855
second protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 236-297 5.36e-41

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: 144.41  E-value: 5.36e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663473103  236 HHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFLLQHIEEPCSLG 297
Cdd:cd20855      1 HHWVHRRKQEGKCKQCGKSFQQKLSFSSKEIVAISCSWCKEAYHNKDSCFNMKKIEEPCNLG 62
C1_DGKzeta_rpt1 cd20849
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase zeta (DAG ...
 153-223 4.04e-36

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: 130.83  E-value: 4.04e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663473103  153 EWSENAINGEHLWLETNVSGDLCYLGEEGCQVK-FSKSAVRRKCAACKIVVHNACMEQLEKINFRCKPTFRE 223
Cdd:cd20849      1 DWSESAVYGEHIWFETNVSGDFCYVGEQNCVAKqLQKSVSRKKCAACKIVVHTPCIEQLEKINFRCKPSFRE 72
C1_DGK_typeIV_rpt1 cd20802
first protein kinase C conserved region 1 (C1 domain) found in type IV diacylglycerol kinases; ...
 158-223 1.47e-35

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: 128.95  E-value: 1.47e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1663473103  158 AINGEHLWLETNVSGDLCYLGEEGCQvkfsKSAVRRKCAACKIVVHNACMEQLEKINFRCKPTFRE 223
Cdd:cd20802      1 AVNGEHLWTDTSASGDLCYVGEQDCL----KSGSRKKCSACKIVVHTGCIPQLEKINFKCKPTFRE 62
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 360-459 2.97e-33

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: 124.62  E-value: 2.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  360 PLLVFVNPKSGGNQGTKVLQMFMWYLNPRQV-FDLSQ-EGPRDALELYRKMPNL---RILACGGDGTVGWILSILDELQl 434
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEDgydRIVVAGGDGTVNEVLNGLAGLA- 79

                           90       100
                   ....*....|....*....|....*
gi 1663473103  435 nPQPPVAVLPLGTGNDLARTLNWGG 459
Cdd:pfam00781   80 -TRPPLGIIPLGTGNDFARALGIPG 103
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 358-683 3.08e-27

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 113.02  E-value: 3.08e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  358 MKPLLVFVNPKSGGNQGTKVLQMFMWYLNpRQVFDLSQ---EGPRDALELYRKMPNL---RILACGGDGTVGWILSILde 431
Cdd:COG1597      2 MMRALLIVNPASGRGRAARLLERLVAALR-AAGLEVEVletESPGDATELAREAAAEgadLVVAAGGDGTVNEVANGL-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  432 lqLNPQPPVAVLPLGTGNDLARTLNwgggyTDEPVAKILCHVEDGAIVQLD------RWnlqvernpdlppkeledgtqk 505
Cdd:COG1597     79 --AGTGPPLGILPLGTGNDFARALG-----IPLDPEAALEALLTGRTRRIDlgrvngRY--------------------- 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  506 lplnvFNNYFSLGFDAHVTLEFHESReanpekfnSRFRNKMFYAGAAFSDFLQRSSRdlskHVKVVCDGTDLtskiqELK 585
Cdd:COG1597    131 -----FLNVAGIGFDAEVVERANRAL--------KRRLGKLAYVLAALRALLRYRPF----RLRIELDGEEI-----EGE 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  586 FQCIVFLNIPRYcaGTMPWGNPGDhrefepqRHDDGFIEVIGFT-------MASLAALQVGGHGE----RLHQCREVTLL 654
Cdd:COG1597    189 ALLVAVGNGPYY--GGGLRLAPDA-------SLDDGLLDVVVVRplsrlrlLRLLPRLLRGRHLRhpgvRYFRAREVEIE 259

                          330       340
                   ....*....|....*....|....*....
gi 1663473103  655 TYKSIPMQVDGEPCRLAPSlIRISLRNQA 683
Cdd:COG1597    260 SDRPLPVQLDGEPLGLATP-LEFEVLPGA 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
924-1041 2.83e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 2.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  924 KKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSelLDMTDSEtGETALHKAACQRHRGICQMLVEAGASLGKMDS 1003
Cdd:COG0666    141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1663473103 1004 KGKTPRDRAQQAGDPDLASYLESHQNYPVVPHEDLETA 1041
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
907-1002 7.60e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 7.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  907 LLQSVIAGDfLRFVEW-CKKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSELLDMtdsetGETALHKAACQRHR 985
Cdd:pfam12796    1 LHLAAKNGN-LELVKLlLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1663473103  986 GICQMLVEAGASLGKMD 1002
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
906-1041 3.51e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.52  E-value: 3.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  906 ALLQSVIAGDFLRFVEWCKKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSelLDMTDSEtGETALHKAACQRHR 985
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD--VNARDKD-GETPLHLAAYNGNL 133

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1663473103  986 GICQMLVEAGASLGKMDSKGKTPRDRAQQAGDPDLASYLESHQNYPVVPHEDLETA 1041
Cdd:COG0666    134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
906-1024 9.14e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 9.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  906 ALLQSVIAGDfLRFVEW-CKKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSelLDMTDSEtGETALHKAACQRH 984
Cdd:COG0666    156 PLHLAAANGN-LEIVKLlLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD--VNAKDND-GKTALDLAAENGN 231

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1663473103  985 RGICQMLVEAGASLGKMDSKGKTPRDRAQQAGDPDLASYL 1024
Cdd:COG0666    232 LEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 236-297 1.84e-10

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: 57.07  E-value: 1.84e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1663473103  236 HHWVHRRRQ-EGKCKQCGKGFQQKFSFHSKeivaiSCSWCKQAFHNKvtCFLLQHIEEpCSLG 297
Cdd:cd20805      1 HHWVEGNLPsGAKCSVCGKKCGSSFGLAGY-----RCSWCKRTVHSE--CIDKLGPEE-CDLG 55
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 236-295 1.12e-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: 52.06  E-value: 1.12e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663473103  236 HHWVHRR-RQEGKCKQCGKgfqqkfSFHSKEIVAISCSWCKQAFHNKvtCFLLQHIEEPCS 295
Cdd:pfam00130    1 HHFVHRNfKQPTFCDHCGE------FLWGLGKQGLKCSWCKLNVHKR--CHEKVPPECGCD 53
PRK13057 PRK13057
lipid kinase;
362-456 2.42e-07

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 53.38  E-value: 2.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  362 LVFVNPKSggNQGTKVLQMFMWYLNPRQvFDLSQEGP------RDALELYRKMPNLRILAcGGDGTVGWILSILDELQLn 435
Cdd:PRK13057     1 LLLVNRHA--RSGRAALAAARAALEAAG-LELVEPPAedpddlSEVIEAYADGVDLVIVG-GGDGTLNAAAPALVETGL- 75

                           90       100
                   ....*....|....*....|.
gi 1663473103  436 pqpPVAVLPLGTGNDLARTLN 456
Cdd:PRK13057    76 ---PLGILPLGTANDLARTLG 93
Ank_4 pfam13637
Ankyrin repeats (many copies);
938-992 5.74e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 5.74e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1663473103  938 SLLHHAAKTGHGEIVKYILEHGSSelLDMTDSEtGETALHKAACQRHRGICQMLV 992
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGAD--INAVDGN-GETALHFAASNGNVEVLKLLL 54
PRK12361 PRK12361
hypothetical protein; Provisional
 359-476 8.51e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 53.09  E-value: 8.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  359 KPLLVFVNPKSGGNQGTKVLQMFMWYLNPRqvFDLS-QEGPRD------ALELYRKMPNLrILACGGDGTVGWILSILde 431
Cdd:PRK12361   243 KRAWLIANPVSGGGKWQEYGEQIQRELKAY--FDLTvKLTTPEisaealAKQARKAGADI-VIACGGDGTVTEVASEL-- 317

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1663473103  432 lqLNPQPPVAVLPLGTGNDLARTLnWGGGYTDEPVAKILCHVEDG 476
Cdd:PRK12361   318 --VNTDITLGIIPLGTANALSHAL-FGLGSKLIPVEQACDNIIQG 359
PRK13054 PRK13054
lipid kinase; Reviewed
 412-453 2.29e-05

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 47.56  E-value: 2.29e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1663473103  412 RILACGGDGTVGWILSILDELQLNPQPPVAVLPLGTGNDLAR 453
Cdd:PRK13054    59 TVIAGGGDGTINEVATALAQLEGDARPALGILPLGTANDFAT 100
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 163-210 3.53e-05

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: 42.43  E-value: 3.53e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1663473103  163 HLWLETNV-SGDLCYLGEEGCQVKFSKSAVRrkCAACKIVVHNACMEQL 210
Cdd:cd20805      1 HHWVEGNLpSGAKCSVCGKKCGSSFGLAGYR--CSWCKRTVHSECIDKL 47
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 236-306 7.21e-05

second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, DAG kinase epsilon, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase epsilon, also called diglyceride kinase epsilon (DGK-epsilon), is the only isoform classified as type III; it possesses a hydrophobic domain in addition to C1 and catalytic domains that are present in all DGKs, and shows selectivity for acyl chains. It is highly selective for arachidonate-containing species of DAG. It may terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition. DAG kinase epsilon contains two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410403  Cd Length: 63  Bit Score: 41.49  E-value: 7.21e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1663473103  236 HHWVHrrrqeG------KCKQCGK--GFQQKFSFHSkeivaisCSWCKQAFHNKvtCflLQHIEEPCSLGAHAAVIIPP 306
Cdd:cd20853      1 HHWVR-----GnlplcsVCCVCNEqcGNQPGLCDYR-------CCWCQRTVHDD--C--LAKLPKECDLGAFRNFIVPP 63
PRK13059 PRK13059
putative lipid kinase; Reviewed
 358-456 1.14e-04

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 45.41  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  358 MKPLLVFVNPKSGGN----QGTKVLQMFMWYLNPRQVFDLSQEGPRD-ALEL----YRkmpnlRILACGGDGTVGWILSI 428
Cdd:PRK13059     1 MKKVKFIYNPYSGENaiisELDKVIRIHQEKGYLVVPYRISLEYDLKnAFKDidesYK-----YILIAGGDGTVDNVVNA 75

                           90       100
                   ....*....|....*....|....*...
gi 1663473103  429 LDELQLNPqpPVAVLPLGTGNDLARTLN 456
Cdd:PRK13059    76 MKKLNIDL--PIGILPVGTANDFAKFLG 101
Ank_5 pfam13857
Ankyrin repeats (many copies);
940-979 2.44e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.44e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1663473103  940 LHHAAKTGHGEIVKYILEHGSSelLDMTDSEtGETALHKA 979
Cdd:pfam13857   20 LHVAAKYGALEIVRVLLAYGVD--LNLKDEE-GLTALDLA 56
PRK13055 PRK13055
putative lipid kinase; Reviewed
 413-456 4.91e-04

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 43.44  E-value: 4.91e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1663473103  413 ILACGGDGTVGWILSILdeLQLNPQPPVAVLPLGTGNDLARTLN 456
Cdd:PRK13055    63 IIAAGGDGTINEVVNGI--APLEKRPKMAIIPAGTTNDYARALK 104
Ank_5 pfam13857
Ankyrin repeats (many copies);
955-1012 7.64e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 7.64e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1663473103  955 ILEHGSsELLDMTDSEtGETALHKAACQRHRGICQMLVEAGASLGKMDSKGKTPRDRA 1012
Cdd:pfam13857    1 LLEHGP-IDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 926-1030 2.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  926 GANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSelLDMTDsETGETALHKAACQRHRGICQMLVEAGASLGKMDSKG 1005
Cdd:PHA02874   114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD--VNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                           90       100
                   ....*....|....*....|....*
gi 1663473103 1006 KTPRDRAQQAGDPDLASYLESHQNY 1030
Cdd:PHA02874   191 ESPLHNAAEYGDYACIKLLIDHGNH 215
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 236-297 2.87e-03

second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the second one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410401  Cd Length: 52  Bit Score: 36.94  E-value: 2.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663473103  236 HHWVhRRRQEGKCKQCGKGFQqkfSFHSkeIVAISCSWCKQAFHNKvtCflLQHIEEPCSLG 297
Cdd:cd20851      1 HHWV-EGNCPGKCDKCHKSIK---SYQG--LTGLHCVWCHITLHNK--C--ASHVKPECDLG 52
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 935-961 3.78e-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: 3.78e-03
                            10        20
                    ....*....|....*....|....*..
gi 1663473103   935 DHCSLLHHAAKTGHGEIVKYILEHGSS 961
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
924-1007 4.13e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663473103  924 KKGANLLIRGPDHCSLLHHAAKTGHGEIVKYILEHGSSELLDMTDsetGETALHKAACQRHRGICQMLVEAGASLGKMDS 1003
Cdd:COG0666    207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD---GLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                   ....
gi 1663473103 1004 KGKT 1007
Cdd:COG0666    284 DLLT 287
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 412-455 4.84e-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: 40.18  E-value: 4.84e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1663473103  412 RILACGGDGTVGWILSILdeLQLNPQPPVAVLPLGTGNDLARTL 455
Cdd:TIGR00147   60 TVIAGGGDGTINEVVNAL--IQLDDIPALGILPLGTANDFARSL 101
Ank_4 pfam13637
Ankyrin repeats (many copies);
974-1024 5.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 5.92e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1663473103  974 TALHKAACQRHRGICQMLVEAGASLGKMDSKGKTPRDRAQQAGDPDLASYL 1024
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
976-1024 7.62e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.63  E-value: 7.62e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1663473103  976 LHKAACQRHRGICQMLVEAGASLGKMDSKGKTPRDRAQQAGDPDLASYL 1024
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 935-959 8.33e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 8.33e-03
                           10        20
                   ....*....|....*....|....*
gi 1663473103  935 DHCSLLHHAAKTGHGEIVKYILEHG 959
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG 25
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 972-1002 9.71e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 9.71e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1663473103  972 GETALHKAACQR-HRGICQMLVEAGASLGKMD 1002
Cdd:pfam00023    2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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