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Conserved domains on  [gi|2055256182|emb|CAD8140463|]
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unnamed protein product [Paramecium octaurelia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 309-460 2.06e-58

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: 196.28  E-value: 2.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 309 NYFGIGLDAKFCYDFHNLRQTSPQLFKSRLGNKLIYTQMGLNDLIKNEKSGLGKKIKVICDDQVIDIPDQVENVIILNIN 388
Cdd:pfam00609   4 NYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPKSLEGIVVLNIP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055256182 389 SWSGGvTGLW----EQDGDFKQQKMNDGLLEIIGVTSILHLGRIQVGLDKPYQLGQGRKIQIIYPSNSYVQIDGEP 460
Cdd:pfam00609  84 SYAGG-TDLWgnskEDGLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 107-160 5.07e-24

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: 95.59  E-value: 5.07e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKV-NQQCDFG 160
Cdd:cd20805     1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLgPEECDLG 55
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 176-274 3.55e-22

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: 92.65  E-value: 3.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 176 PIIVVINQKSGGQVGVDFYKSFLRFLNPIQV-LNIQEMHK-------LKNFTHIKTAKLITAGGDGTVASVINYIKEFDW 247
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGpgdalelAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLAT 80

                          90       100
                  ....*....|....*....|....*..
gi 2055256182 248 NPPIAILPLGTGNDLSRALGWGGTYEQ 274
Cdd:pfam00781  81 RPPLGIIPLGTGNDFARALGIPGDPEE 107
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 46-91 2.77e-08

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: 50.59  E-value: 2.77e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2055256182  46 HSYAESKSSGLLFCNVCKKLLFSLWgAQYHECLICGIYVHKKCRRN 91
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGLF-KQGLKCSDCGLVCHKKCLDK 45
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 540-777 1.19e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 55.51  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 540 KQYEKRRQRLLSEyndllnKKSEETQIhqKSQSPEDKQEDLTTSRiNDKLLKMKKFQQNQREQQLIQYSYKEQLIETRRK 619
Cdd:pfam17380 405 KILEEERQRKIQQ------QKVEMEQI--RAEQEEARQREVRRLE-EERAREMERVRLEEQERQQQVERLRQQEEERKRK 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 620 QISSERELRAfQKEVQDTSR--LEQVQRNRDmiQKLITDKQvKRRMsydaklqkweLLKQAQyliPRSTRVDETLARYQK 697
Cdd:pfam17380 476 KLELEKEKRD-RKRAEEQRRkiLEKELEERK--QAMIEEER-KRKL----------LEKEME---ERQKAIYEEERRREA 538

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 698 CLEDKKQQDMQRLKRLEESLEKACSKKTQNIVEIKRRGLLEQLKIEEalfnRARSQNARNTNILEKAPqktvLIRPSMSE 777
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE----KARAEYEATTPITTIKP----IYRPRISE 610
 
Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 309-460 2.06e-58

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: 196.28  E-value: 2.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 309 NYFGIGLDAKFCYDFHNLRQTSPQLFKSRLGNKLIYTQMGLNDLIKNEKSGLGKKIKVICDDQVIDIPDQVENVIILNIN 388
Cdd:pfam00609   4 NYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPKSLEGIVVLNIP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055256182 389 SWSGGvTGLW----EQDGDFKQQKMNDGLLEIIGVTSILHLGRIQVGLDKPYQLGQGRKIQIIYPSNSYVQIDGEP 460
Cdd:pfam00609  84 SYAGG-TDLWgnskEDGLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 309-460 3.84e-43

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: 153.64  E-value: 3.84e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  309 NYFGIGLDAKFCYDFHNLRQTSPQLFKSRLGNKLIYTQMGLNDLIKNEKSGLGKKIKVICDDQVIDIPDQVENVIILNIN 388
Cdd:smart00045   4 NYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPNSLEGIAVLNIP 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055256182  389 SWSGGvTGLW----EQDGDFKQQKMNDGLLEIIGVTSILHLGRIQVGLDKPYQLGQGRKIQIIYPSNSY--VQIDGEP 460
Cdd:smart00045  84 SYGGG-TNLWgttdKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSKTipMQVDGEP 160
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 107-160 5.07e-24

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: 95.59  E-value: 5.07e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKV-NQQCDFG 160
Cdd:cd20805     1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLgPEECDLG 55
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 176-274 3.55e-22

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: 92.65  E-value: 3.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 176 PIIVVINQKSGGQVGVDFYKSFLRFLNPIQV-LNIQEMHK-------LKNFTHIKTAKLITAGGDGTVASVINYIKEFDW 247
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGpgdalelAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLAT 80

                          90       100
                  ....*....|....*....|....*..
gi 2055256182 248 NPPIAILPLGTGNDLSRALGWGGTYEQ 274
Cdd:pfam00781  81 RPPLGIIPLGTGNDFARALGIPGDPEE 107
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 226-467 1.75e-21

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 95.69  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 226 LITAGGDGTVASVINYIKEFDwnPPIAILPLGTGNDLSRALGWGgtyeqLDASHVLSKIMNNEnVTLLDrwnV-KIGNKN 304
Cdd:COG1597    62 VVAAGGDGTVNEVANGLAGTG--PPLGILPLGTGNDFARALGIP-----LDPEAALEALLTGR-TRRID---LgRVNGRY 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 305 FklFNYFGIGLDAKFCYDFHNLRqtspqlfKSRLGnKLIYTQMGLNDLIKNEksglGKKIKVICDDQVIDIPdqVENVII 384
Cdd:COG1597   131 F--LNVAGIGFDAEVVERANRAL-------KRRLG-KLAYVLAALRALLRYR----PFRLRIELDGEEIEGE--ALLVAV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 385 LNINSWSGGVTGLWEQDgdfkqqkMNDGLLEIIGVTSILHLGRIQVGL---------DKPYQLGQGRKIQIIYPSNSYVQ 455
Cdd:COG1597   195 GNGPYYGGGLRLAPDAS-------LDDGLLDVVVVRPLSRLRLLRLLPrllrgrhlrHPGVRYFRAREVEIESDRPLPVQ 267

                         250
                  ....*....|..
gi 2055256182 456 IDGEPLSIGPSI 467
Cdd:COG1597   268 LDGEPLGLATPL 279
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 178-295 2.00e-21

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: 90.43  E-value: 2.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  178 IVVINQKSGGQVGVDFYKSFLRFLNPIQVLNIQE------MHKLKNFTHIKTakLITAGGDGTVASVINYIKEFDW---N 248
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKkgpavaLVIFRDVPDFNR--VLVCGGDGTVGWVLNALDKRELplpE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2055256182  249 PPIAILPLGTGNDLSRALGWGGTYEQLDASHVLSKIMNNEnVTLLDR 295
Cdd:smart00046  79 PPVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESD-TVKLDR 124
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 222-471 4.12e-11

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: 64.83  E-value: 4.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 222 KTAKLITAGGDGTVASVINYIKEFDWNPPIAILPLGTGNDLSRALgwgGTYEQLDAShvLSKIMNNENVTlldrwnVKIG 301
Cdd:TIGR00147  57 GVDTVIAGGGDGTINEVVNALIQLDDIPALGILPLGTANDFARSL---GIPEDLDKA--AKLVIAGDARA------IDMG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 302 --NKNFKLFNYFGIGLDAKFCYDFhnlrqtsPQLFKSRLGnKLIYTQMGLndliknEKSGLGKKIKVIC--DDQVIdipd 377
Cdd:TIGR00147 126 qvNKQYCFINMAGGGFGTEITTET-------PEKLKAALG-SLSYILSGL------MRMDTLQPFRCEIrgEGEHW---- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 378 QVENVIILNINSwsggvtglwEQDGDFKQ----QKMNDGLLEIIGVTSILHLGRIQVGLDKpyQLGQGRKIQ-IIYPSNS 452
Cdd:TIGR00147 188 QGEAVVFLVGNG---------RQAGGGQKlapdASINDGLLDLRIFTNDNLLPALVLTLMS--DEGKHTDNPnIIYGKAS 256

                         250       260
                  ....*....|....*....|....*....
gi 2055256182 453 YVQI----------DGEPLSIGPSIIDIS 471
Cdd:TIGR00147 257 RIDIqtphkitfnlDGEPLGGTPFHIEIL 285
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 107-157 1.84e-10

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 56.71  E-value: 1.84e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2055256182  107 HQWLSGNLPMNSICCHCGLTCGyFFDLEGKSCLWCQKVVHEECKDKVNQQC 157
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIW-GSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 107-160 4.54e-10

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: 55.91  E-value: 4.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCgYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFG 160
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFL-WGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
PRK13059 PRK13059
putative lipid kinase; Reviewed
 226-417 6.21e-10

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 61.21  E-value: 6.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 226 LITAGGDGTVASVINYIKEFDWNPPIAILPLGTGNDLSRALGWGGtyeqlDASHVLSKIMNNENVtlldrwNVKIGNKNF 305
Cdd:PRK13059   60 ILIAGGDGTVDNVVNAMKKLNIDLPIGILPVGTANDFAKFLGMPT-----DIGEACEQILKSKPK------KVDLGKIND 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 306 KLF-NYFGIGLdakfcydFHNLRQTSPQLFKSRLGnKLIYTQMGLNDLIKNEKSglgkKIKVICDDQVIDipDQVENVII 384
Cdd:PRK13059  129 KYFiNVASTGL-------FTDVSQKTDVNLKNTIG-KLAYYLKGLEELPNFRKL----KVKVTSEEVNFD--GDMYLMLV 194

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2055256182 385 LNinswsggvtglWEQDGDFK---QQKMNDGLLEII 417
Cdd:PRK13059  195 FN-----------GQTAGNFNlayKAEVDDGLLDVI 219
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 46-91 2.77e-08

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: 50.59  E-value: 2.77e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2055256182  46 HSYAESKSSGLLFCNVCKKLLFSLWgAQYHECLICGIYVHKKCRRN 91
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGLF-KQGLKCSDCGLVCHKKCLDK 45
PRK13337 PRK13337
putative lipid kinase; Reviewed
 226-267 3.75e-08

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 55.82  E-value: 3.75e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2055256182 226 LITAGGDGTVASVINYIKEFDWNPPIAILPLGTGNDLSRALG 267
Cdd:PRK13337   61 VIAAGGDGTLNEVVNGIAEKENRPKLGIIPVGTTNDFARALH 102
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 540-777 1.19e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 55.51  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 540 KQYEKRRQRLLSEyndllnKKSEETQIhqKSQSPEDKQEDLTTSRiNDKLLKMKKFQQNQREQQLIQYSYKEQLIETRRK 619
Cdd:pfam17380 405 KILEEERQRKIQQ------QKVEMEQI--RAEQEEARQREVRRLE-EERAREMERVRLEEQERQQQVERLRQQEEERKRK 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 620 QISSERELRAfQKEVQDTSR--LEQVQRNRDmiQKLITDKQvKRRMsydaklqkweLLKQAQyliPRSTRVDETLARYQK 697
Cdd:pfam17380 476 KLELEKEKRD-RKRAEEQRRkiLEKELEERK--QAMIEEER-KRKL----------LEKEME---ERQKAIYEEERRREA 538

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 698 CLEDKKQQDMQRLKRLEESLEKACSKKTQNIVEIKRRGLLEQLKIEEalfnRARSQNARNTNILEKAPqktvLIRPSMSE 777
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE----KARAEYEATTPITTIKP----IYRPRISE 610
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 540-770 8.85e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 8.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 540 KQYEKRRQRLLSEyNDLLNKKSEETQIHQKSQSPEDKQEDLTTSRINDKLLKMKKFQQNQRE--QQLIQysYKEQLIETR 617
Cdd:COG1196   267 AELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleEELEE--LEEELEELE 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 618 RKQISSERELRAFQKEVQDT-SRLEQVQRNRDMIQKLITDKQVKRRmsyDAKLQKWELLKQAQYLIPRSTRVDETLARYQ 696
Cdd:COG1196   344 EELEEAEEELEEAEAELAEAeEALLEAEAELAEAEEELEELAEELL---EALRAAAELAAQLEELEEAEEALLERLERLE 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055256182 697 KCLEDKKQQDmQRLKRLEESLEKACSKKTQNIVEIKRRGLLEQLKIEEALFNRARSQNARNTNILEKAPQKTVL 770
Cdd:COG1196   421 EELEELEEAL-AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 46-91 1.87e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 45.54  E-value: 1.87e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2055256182   46 HSYAESKSSGLLFCNVCKKllfSLWGAQYH--ECLICGIYVHKKCRRN 91
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRK---SIWGSFKQglRCSECKVKCHKKCADK 45
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 58-91 2.80e-05

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: 42.43  E-value: 2.80e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2055256182  58 FCNVCKKLLFSLWGAQYHeCLICGIYVHKKCRRN 91
Cdd:pfam00130  13 FCDHCGEFLWGLGKQGLK-CSWCKLNVHKRCHEK 45
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 543-756 4.20e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  543 EKRRQRLLSEYNDLLNKKSEE-----TQIHQKSQSPEDKQEDL--TTSRINDkLLKMKKFQQNQREQQLIQYSYKE-QLI 614
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKleelrLEVSELEEEIEELQKELyaLANEISR-LEQQKQILRERLANLERQLEELEaQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  615 ETRRKQISSERELRAFQKEvqdtsrLEQVQRNRDMIQKLITDKQVKRRMS---YDAKLQKWE--------LLKQAQYLIP 683
Cdd:TIGR02168  327 ELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELesrLEELEEQLEtlrskvaqLELQIASLNN 400

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055256182  684 RSTRVDETLARyqkcLEDKKQQDMQRLKRLEESLEKACSKKTQNIVEIKRRGLLEQLKIEEALFNRARSQNAR 756
Cdd:TIGR02168  401 EIERLEARLER----LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
PRK00106 PRK00106
ribonuclease Y;
498-638 8.04e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 39.85  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 498 EEQNHITKQAKDEIVNHllplkKIKVPPEYENDSQFYQETIMKQYEKRRQRL------LSEYNDLLNKK-----SEETQI 566
Cdd:PRK00106   53 RDAEHIKKTAKRESKAL-----KKELLLEAKEEARKYREEIEQEFKSERQELkqiesrLTERATSLDRKdenlsSKEKTL 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055256182 567 HQKSQSPEDKQEDLTTSRINDKLLKMKKFQQNQREQQLIQYSYKEQLIETRRKQISSE--RELRAFQKEVQDTS 638
Cdd:PRK00106  128 ESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEiaTRIREAEREVKDRS 201
 
Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 309-460 2.06e-58

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: 196.28  E-value: 2.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 309 NYFGIGLDAKFCYDFHNLRQTSPQLFKSRLGNKLIYTQMGLNDLIKNEKSGLGKKIKVICDDQVIDIPDQVENVIILNIN 388
Cdd:pfam00609   4 NYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPKSLEGIVVLNIP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055256182 389 SWSGGvTGLW----EQDGDFKQQKMNDGLLEIIGVTSILHLGRIQVGLDKPYQLGQGRKIQIIYPSNSYVQIDGEP 460
Cdd:pfam00609  84 SYAGG-TDLWgnskEDGLGFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 309-460 3.84e-43

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: 153.64  E-value: 3.84e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  309 NYFGIGLDAKFCYDFHNLRQTSPQLFKSRLGNKLIYTQMGLNDLIKNEKSGLGKKIKVICDDQVIDIPDQVENVIILNIN 388
Cdd:smart00045   4 NYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPNSLEGIAVLNIP 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055256182  389 SWSGGvTGLW----EQDGDFKQQKMNDGLLEIIGVTSILHLGRIQVGLDKPYQLGQGRKIQIIYPSNSY--VQIDGEP 460
Cdd:smart00045  84 SYGGG-TNLWgttdKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSKTipMQVDGEP 160
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 107-160 5.07e-24

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: 95.59  E-value: 5.07e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKV-NQQCDFG 160
Cdd:cd20805     1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLgPEECDLG 55
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 176-274 3.55e-22

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: 92.65  E-value: 3.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 176 PIIVVINQKSGGQVGVDFYKSFLRFLNPIQV-LNIQEMHK-------LKNFTHIKTAKLITAGGDGTVASVINYIKEFDW 247
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGpgdalelAREAAEDGYDRIVVAGGDGTVNEVLNGLAGLAT 80

                          90       100
                  ....*....|....*....|....*..
gi 2055256182 248 NPPIAILPLGTGNDLSRALGWGGTYEQ 274
Cdd:pfam00781  81 RPPLGIIPLGTGNDFARALGIPGDPEE 107
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 226-467 1.75e-21

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 95.69  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 226 LITAGGDGTVASVINYIKEFDwnPPIAILPLGTGNDLSRALGWGgtyeqLDASHVLSKIMNNEnVTLLDrwnV-KIGNKN 304
Cdd:COG1597    62 VVAAGGDGTVNEVANGLAGTG--PPLGILPLGTGNDFARALGIP-----LDPEAALEALLTGR-TRRID---LgRVNGRY 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 305 FklFNYFGIGLDAKFCYDFHNLRqtspqlfKSRLGnKLIYTQMGLNDLIKNEksglGKKIKVICDDQVIDIPdqVENVII 384
Cdd:COG1597   131 F--LNVAGIGFDAEVVERANRAL-------KRRLG-KLAYVLAALRALLRYR----PFRLRIELDGEEIEGE--ALLVAV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 385 LNINSWSGGVTGLWEQDgdfkqqkMNDGLLEIIGVTSILHLGRIQVGL---------DKPYQLGQGRKIQIIYPSNSYVQ 455
Cdd:COG1597   195 GNGPYYGGGLRLAPDAS-------LDDGLLDVVVVRPLSRLRLLRLLPrllrgrhlrHPGVRYFRAREVEIESDRPLPVQ 267

                         250
                  ....*....|..
gi 2055256182 456 IDGEPLSIGPSI 467
Cdd:COG1597   268 LDGEPLGLATPL 279
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 178-295 2.00e-21

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: 90.43  E-value: 2.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  178 IVVINQKSGGQVGVDFYKSFLRFLNPIQVLNIQE------MHKLKNFTHIKTakLITAGGDGTVASVINYIKEFDW---N 248
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKkgpavaLVIFRDVPDFNR--VLVCGGDGTVGWVLNALDKRELplpE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2055256182  249 PPIAILPLGTGNDLSRALGWGGTYEQLDASHVLSKIMNNEnVTLLDR 295
Cdd:smart00046  79 PPVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDALESD-TVKLDR 124
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 107-169 2.63e-20

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: 85.02  E-value: 2.63e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFGEFKDAIILP 169
Cdd:cd20853     1 HHWVRGNLPLCSVCCVCNEQCGNQPGLCDYRCCWCQRTVHDDCLAKLPKECDLGAFRNFIVPP 63
C1_DGK_typeII_rpt2 cd20852
second protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 107-160 2.81e-16

second protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. 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: 410402  Cd Length: 54  Bit Score: 73.51  E-value: 2.81e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFG 160
Cdd:cd20852     1 HQWLEGNLPVSSKCAVCDKTCGSVLRLQDWRCLWCGATVHTACKDSLPTKCSLG 54
C1_DGKdelta_rpt2 cd20893
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
 107-161 4.14e-14

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta (DAG kinase delta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase delta, also called 130 kDa diacylglycerol kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. DAG kinase delta 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: 410443  Cd Length: 61  Bit Score: 67.40  E-value: 4.14e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFGE 161
Cdd:cd20893     6 HQWLEGNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKELLLTKCPLGQ 60
C1_DGKeta_rpt2 cd20894
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 107-163 1.15e-13

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG kinase eta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. It is classified as a type II DAG kinase (DGK), containing pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. The diacylglycerol kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase eta 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: 410444  Cd Length: 62  Bit Score: 66.46  E-value: 1.15e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFGEFK 163
Cdd:cd20894     6 HQWLEGNLPVSAKCSVCDKTCGSVLRLQDWRCLWCKAMVHTACKDQYPRKCPLGQCR 62
C1_DGKtheta_typeV_rpt3 cd20854
third protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 107-169 3.21e-11

third protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the third 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: 410404  Cd Length: 63  Bit Score: 59.20  E-value: 3.21e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFGEFKDaIILP 169
Cdd:cd20854     1 HHWREGNLPSNSKCEVCKKSCGSSECLAGMRCEWCGITAHASCYKSLPKECNFGRLRN-IILP 62
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 222-471 4.12e-11

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: 64.83  E-value: 4.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 222 KTAKLITAGGDGTVASVINYIKEFDWNPPIAILPLGTGNDLSRALgwgGTYEQLDAShvLSKIMNNENVTlldrwnVKIG 301
Cdd:TIGR00147  57 GVDTVIAGGGDGTINEVVNALIQLDDIPALGILPLGTANDFARSL---GIPEDLDKA--AKLVIAGDARA------IDMG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 302 --NKNFKLFNYFGIGLDAKFCYDFhnlrqtsPQLFKSRLGnKLIYTQMGLndliknEKSGLGKKIKVIC--DDQVIdipd 377
Cdd:TIGR00147 126 qvNKQYCFINMAGGGFGTEITTET-------PEKLKAALG-SLSYILSGL------MRMDTLQPFRCEIrgEGEHW---- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 378 QVENVIILNINSwsggvtglwEQDGDFKQ----QKMNDGLLEIIGVTSILHLGRIQVGLDKpyQLGQGRKIQ-IIYPSNS 452
Cdd:TIGR00147 188 QGEAVVFLVGNG---------RQAGGGQKlapdASINDGLLDLRIFTNDNLLPALVLTLMS--DEGKHTDNPnIIYGKAS 256

                         250       260
                  ....*....|....*....|....*....
gi 2055256182 453 YVQI----------DGEPLSIGPSIIDIS 471
Cdd:TIGR00147 257 RIDIqtphkitfnlDGEPLGGTPFHIEIL 285
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 107-157 1.84e-10

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 56.71  E-value: 1.84e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2055256182  107 HQWLSGNLPMNSICCHCGLTCGyFFDLEGKSCLWCQKVVHEECKDKVNQQC 157
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIW-GSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 107-160 4.54e-10

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: 55.91  E-value: 4.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCgYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFG 160
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFL-WGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
PRK13059 PRK13059
putative lipid kinase; Reviewed
 226-417 6.21e-10

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 61.21  E-value: 6.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 226 LITAGGDGTVASVINYIKEFDWNPPIAILPLGTGNDLSRALGWGGtyeqlDASHVLSKIMNNENVtlldrwNVKIGNKNF 305
Cdd:PRK13059   60 ILIAGGDGTVDNVVNAMKKLNIDLPIGILPVGTANDFAKFLGMPT-----DIGEACEQILKSKPK------KVDLGKIND 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 306 KLF-NYFGIGLdakfcydFHNLRQTSPQLFKSRLGnKLIYTQMGLNDLIKNEKSglgkKIKVICDDQVIDipDQVENVII 384
Cdd:PRK13059  129 KYFiNVASTGL-------FTDVSQKTDVNLKNTIG-KLAYYLKGLEELPNFRKL----KVKVTSEEVNFD--GDMYLMLV 194

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2055256182 385 LNinswsggvtglWEQDGDFK---QQKMNDGLLEII 417
Cdd:PRK13059  195 FN-----------GQTAGNFNlayKAEVDDGLLDVI 219
C1_DGKgamma_rpt2 cd20892
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
 107-169 9.34e-10

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma (DAG kinase gamma) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DGK-gamma contains two copies of the C1 domain. This model corresponds to the second one. DGK-gamma contains 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: 410442  Cd Length: 61  Bit Score: 55.20  E-value: 9.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCgyFFDLEGKSCLWCQKVVHEECKDKVNQQCDFGEFKDAIILP 169
Cdd:cd20892     1 HVWVEGNSPVKCDRCHKSIKC--YQGLTGLHCVWCQITLHNKCASHVSPECDGGQLKDHILLP 61
C1_DGKalpha_rpt2 cd20890
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha ...
 107-169 3.33e-09

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha (DAG kinase alpha) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase alpha, also called 80 kDa diacylglycerol kinase, or diglyceride kinase alpha (DGK-alpha), converts the second messenger diacylglycerol into phosphatidate upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase alpha 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: 410440  Cd Length: 62  Bit Score: 53.70  E-value: 3.33e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055256182 107 HQWLSGNLPMNSiCCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFGEFKDAIILP 169
Cdd:cd20890     1 HVWVSGGCESSK-CDKCQKKIKSFQSLTGLHCVWCHLKRHDECLSSVPSTCDCGPLRDHILPP 62
C1_DGKbeta_rpt2 cd20891
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta ...
 107-164 7.30e-09

second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase beta contains two copies of the C1 domain. This model corresponds to the second one. DGK-beta contains 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: 410441  Cd Length: 59  Bit Score: 52.68  E-value: 7.30e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCgyFFDLEGKSCLWCQKVVHEECKDKVNQQCDFGEFKD 164
Cdd:cd20891     3 HFWVEGNCPTKCDKCHKTIKC--YQGLTGLHCVWCQITLHNKCASHVKPECDCGPLKD 58
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 46-91 2.77e-08

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: 50.59  E-value: 2.77e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2055256182  46 HSYAESKSSGLLFCNVCKKLLFSLWgAQYHECLICGIYVHKKCRRN 91
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGLF-KQGLKCSDCGLVCHKKCLDK 45
PRK13337 PRK13337
putative lipid kinase; Reviewed
 226-267 3.75e-08

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 55.82  E-value: 3.75e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2055256182 226 LITAGGDGTVASVINYIKEFDWNPPIAILPLGTGNDLSRALG 267
Cdd:PRK13337   61 VIAAGGDGTLNEVVNGIAEKENRPKLGIIPVGTTNDFARALH 102
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 540-777 1.19e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 55.51  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 540 KQYEKRRQRLLSEyndllnKKSEETQIhqKSQSPEDKQEDLTTSRiNDKLLKMKKFQQNQREQQLIQYSYKEQLIETRRK 619
Cdd:pfam17380 405 KILEEERQRKIQQ------QKVEMEQI--RAEQEEARQREVRRLE-EERAREMERVRLEEQERQQQVERLRQQEEERKRK 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 620 QISSERELRAfQKEVQDTSR--LEQVQRNRDmiQKLITDKQvKRRMsydaklqkweLLKQAQyliPRSTRVDETLARYQK 697
Cdd:pfam17380 476 KLELEKEKRD-RKRAEEQRRkiLEKELEERK--QAMIEEER-KRKL----------LEKEME---ERQKAIYEEERRREA 538

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 698 CLEDKKQQDMQRLKRLEESLEKACSKKTQNIVEIKRRGLLEQLKIEEalfnRARSQNARNTNILEKAPqktvLIRPSMSE 777
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE----KARAEYEATTPITTIKP----IYRPRISE 610
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 107-160 1.25e-07

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: 48.88  E-value: 1.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055256182 107 HQWLSGNLPMNsiCCHCGLTCGYFFDLEGKSCLWCQKVVHEECKDKVNQQCDFG 160
Cdd:cd20851     1 HHWVEGNCPGK--CDKCHKSIKSYQGLTGLHCVWCHITLHNKCASHVKPECDLG 52
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 540-770 8.85e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 8.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 540 KQYEKRRQRLLSEyNDLLNKKSEETQIHQKSQSPEDKQEDLTTSRINDKLLKMKKFQQNQRE--QQLIQysYKEQLIETR 617
Cdd:COG1196   267 AELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleEELEE--LEEELEELE 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 618 RKQISSERELRAFQKEVQDT-SRLEQVQRNRDMIQKLITDKQVKRRmsyDAKLQKWELLKQAQYLIPRSTRVDETLARYQ 696
Cdd:COG1196   344 EELEEAEEELEEAEAELAEAeEALLEAEAELAEAEEELEELAEELL---EALRAAAELAAQLEELEEAEEALLERLERLE 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055256182 697 KCLEDKKQQDmQRLKRLEESLEKACSKKTQNIVEIKRRGLLEQLKIEEALFNRARSQNARNTNILEKAPQKTVL 770
Cdd:COG1196   421 EELEELEEAL-AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
PRK13055 PRK13055
putative lipid kinase; Reviewed
 226-266 9.51e-07

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 51.91  E-value: 9.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2055256182 226 LITAGGDGTVASVINYIKEFDWNPPIAILPLGTGNDLSRAL 266
Cdd:PRK13055   63 IIAAGGDGTINEVVNGIAPLEKRPKMAIIPAGTTNDYARAL 103
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 107-157 1.02e-06

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: 46.36  E-value: 1.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2055256182 107 HQWLSGNLPMNSICCHCGLTCgYFFDLEGKSCLWCQKVVHEECKDKVNQQC 157
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLI-WGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 46-91 1.87e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 45.54  E-value: 1.87e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2055256182   46 HSYAESKSSGLLFCNVCKKllfSLWGAQYH--ECLICGIYVHKKCRRN 91
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRK---SIWGSFKQglRCSECKVKCHKKCADK 45
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 58-91 2.80e-05

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: 42.43  E-value: 2.80e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2055256182  58 FCNVCKKLLFSLWGAQYHeCLICGIYVHKKCRRN 91
Cdd:pfam00130  13 FCDHCGEFLWGLGKQGLK-CSWCKLNVHKRCHEK 45
C1_DGKtheta_typeV_rpt2 cd20804
second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 46-89 3.03e-05

second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three 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: 410354  Cd Length: 57  Bit Score: 42.29  E-value: 3.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2055256182  46 HSYAESKSSGLLFCNVCKKLLFSLWGaqyHECLICGIYVHKKCR 89
Cdd:cd20804     6 HCWSEPGHSKRKFCNVCRKRLEDSPA---FRCEVCEYYVHSDCQ 46
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
 45-88 3.68e-05

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, 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: 410381  Cd Length: 58  Bit Score: 41.94  E-value: 3.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2055256182  45 EHSYAESKSSGLLFCNVCKKLLFSLWGAQYHECLICGIYVHKKC 88
Cdd:cd20831     5 DHTFVATHFKGGPSCAVCNKLIPGRFGKQGYQCRDCGLICHKRC 48
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 543-756 4.20e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  543 EKRRQRLLSEYNDLLNKKSEE-----TQIHQKSQSPEDKQEDL--TTSRINDkLLKMKKFQQNQREQQLIQYSYKE-QLI 614
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKleelrLEVSELEEEIEELQKELyaLANEISR-LEQQKQILRERLANLERQLEELEaQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  615 ETRRKQISSERELRAFQKEvqdtsrLEQVQRNRDMIQKLITDKQVKRRMS---YDAKLQKWE--------LLKQAQYLIP 683
Cdd:TIGR02168  327 ELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELesrLEELEEQLEtlrskvaqLELQIASLNN 400

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055256182  684 RSTRVDETLARyqkcLEDKKQQDMQRLKRLEESLEKACSKKTQNIVEIKRRGLLEQLKIEEALFNRARSQNAR 756
Cdd:TIGR02168  401 EIERLEARLER----LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 563-756 4.57e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 563 ETQIHQKSQSPEDKQEDLTT-----SRINDKLLKMKKfQQNQREQQLI----QYSYKEQLIETRRKQISSERE-----LR 628
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAaqaelDALQAELEELNE-EYNELQAELEalqaEIDKLQAEIAEAEAEIEERREelgerAR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 629 AFQKEVQDTSRLEQVQRNR---DMIQKLITdkqVKRRMSYDAKLQkwELLKQAQyliprstrvdETLARYQKCLEDKKQQ 705
Cdd:COG3883    94 ALYRSGGSVSYLDVLLGSEsfsDFLDRLSA---LSKIADADADLL--EELKADK----------AELEAKKAELEAKLAE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2055256182 706 DMQRLKRLEESLEKACSKKTQniveikRRGLLEQLKIEEALFNRARSQNAR 756
Cdd:COG3883   159 LEALKAELEAAKAELEAQQAE------QEALLAQLSAEEAAAEAQLAELEA 203
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 57-96 5.16e-05

first 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 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: 410351  Cd Length: 54  Bit Score: 41.53  E-value: 5.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2055256182  57 LFCNVCKKLLFSlwGAQyheCLICGIYVHKKCRR---NQIQCK 96
Cdd:cd20801    16 TYCSVCETLILS--GAF---CDCCGLCVDEGCLRkadKRFPCK 53
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 58-88 9.43e-05

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. 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: 410385  Cd Length: 64  Bit Score: 40.91  E-value: 9.43e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2055256182  58 FCNVCKKLLFSLWGAQYHECLICGIYVHKKC 88
Cdd:cd20835    22 YCSHCKDFIWGVIGKQGYQCQVCTCVVHKRC 52
PRK13057 PRK13057
lipid kinase;
226-267 1.01e-04

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 45.29  E-value: 1.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2055256182 226 LITAGGDGTVASVINYIkeFDWNPPIAILPLGTGNDLSRALG 267
Cdd:PRK13057   54 VIVGGGDGTLNAAAPAL--VETGLPLGILPLGTANDLARTLG 93
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 487-764 1.62e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.35  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  487 ENRFLKTMDWAEEQNHITKQAKDEIVNHLLPLKKIKVPPEYENDSQFYQETIMKQYEKRRQRLLSEYNDLLNKKSEETQI 566
Cdd:pfam02463  172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  567 HQKSQSPEDKQEDLTTSRINDKLLKMKKFQQNQREQQLiqysykeqLIETRRKQISSERElrafQKEVQDTSRLEQVQRN 646
Cdd:pfam02463  252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK--------LLAKEEEELKSELL----KLERRKVDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  647 RDMIQKLitDKQVKRRMSYDAKLQKWELLKQAQYlIPRSTRVDETLARYQKcLEDKKQQDMQRLKRLEESLEKACSKKTQ 726
Cdd:pfam02463  320 EKEKKKA--EKELKKEKEEIEELEKELKELEIKR-EAEEEEEEELEKLQEK-LEQLEEELLAKKKLESERLSSAAKLKEE 395

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2055256182  727 -----NIVEIKRRGLLEQLKIEEALFNRARSQNARNTNILEKA 764
Cdd:pfam02463  396 elelkSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEES 438
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 559-788 1.96e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 559 KKSEETQIHQKSQSPEDKQEDLttsrinDKLLKMKKFQQNQREQQLIQYSYKEQLIETRRKQIS-SERELRAFQKEVQDT 637
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKEL------AALKKEEKALLKQLAALERRIAALARRIRALEQELAaLEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 638 SRleQVQRNRDMIQKLITDKQVKRRMSYDAKLQKWELLKQAQylipRSTRVDETLARYQKCLEDKKQQDMQRLKRLEESL 717
Cdd:COG4942    96 RA--ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELAALRAEL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 718 EKACSKKTQNIVEIK------------RRGLLEQLKIEEALFNRARSQNARNTNILEKAPQKTVLIRPSMSEIPQQKPFP 785
Cdd:COG4942   170 EAERAELEALLAELEeeraalealkaeRQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249


                  ...
gi 2055256182 786 QPK 788
Cdd:COG4942   250 ALK 252
PRK13054 PRK13054
lipid kinase; Reviewed
 220-267 3.18e-04

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 43.71  E-value: 3.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2055256182 220 HIKTAKLITAGGDGT---VASVINYIKEfDWNPPIAILPLGTGNDLSRALG 267
Cdd:PRK13054   54 ALGVATVIAGGGDGTineVATALAQLEG-DARPALGILPLGTANDFATAAG 103
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
 44-88 3.91e-04

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. This model describes the C1 domain. 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: 410361  Cd Length: 49  Bit Score: 38.82  E-value: 3.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2055256182  44 LEHSYAESKSSGLLFCNVCKKLLFslWGaqyHECLICGIYVHKKC 88
Cdd:cd20811     1 ISHNFVRKTFFTLAFCDVCRKLLF--QG---FRCQTCGFKFHQRC 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 543-752 5.45e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 5.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  543 EKRRQRLLSEYNDLLNKKSE-ETQIHQKSQSPEDKQEDLTTS---------RINDKLLKMKKFQQNQREQQLIQYSYKEQ 612
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEElEAQLEELESKLDELAEELAELeekleelkeELESLEAELEELEAELEELESRLEELEEQ 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182  613 LIETRRKQISSERELRAFQKEVQD-TSRLEQVQRNRdmiqklitDKQVKRRMSYDAKLQKWELLKQAQylipRSTRVDET 691
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERlEARLERLEDRR--------ERLQQEIEELLKKLEEAELKELQA----ELEELEEE 448

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055256182  692 LARYQKCLEDKKqqdmQRLKRLEESLEKACSKKTQNIVEIKRrgLLEQLKIEEALFNRARS 752
Cdd:TIGR02168  449 LEELQEELERLE----EALEELREELEEAEQALDAAERELAQ--LQARLDSLERLQENLEG 503
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
 59-96 5.97e-04

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. 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: 410360  Cd Length: 52  Bit Score: 38.39  E-value: 5.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2055256182  59 CNVCKKLLfslWGAQY--HECLICGIYVHKKCRRNQIQCK 96
Cdd:cd20810    16 CSVCKKLL---KGLFFqgYKCSVCGAAVHKECIAKVKRCG 52
PRK12361 PRK12361
hypothetical protein; Provisional
 175-269 1.01e-03

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 42.69  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 175 KPIIVVINQKSGGQVGVDFYKSFLRFLNPIQVLNIQEMHKLKNFTHI-KTAK------LITAGGDGT---VASVInyike 244
Cdd:PRK12361  243 KRAWLIANPVSGGGKWQEYGEQIQRELKAYFDLTVKLTTPEISAEALaKQARkagadiVIACGGDGTvteVASEL----- 317

                          90       100
                  ....*....|....*....|....*.
gi 2055256182 245 FDWNPPIAILPLGTGNDLSRAL-GWG 269
Cdd:PRK12361  318 VNTDITLGIIPLGTANALSHALfGLG 343
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 58-97 2.05e-03

second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase family; The diacylglycerol kinase (DGK, EC 2.7.1.107) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity to each isozyme. They have been classified into five types (I-V), according to domain architecture and some common features. All DGK isozymes, except for DGKtheta, contain two copies of the C1 domain. This model corresponds to the second one. DGKtheta harbors three C1 domains. Its third C1 domain is included here. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410355  Cd Length: 55  Bit Score: 37.04  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2055256182  58 FCNVCKKLLFSLWGAQYHECLICGIYVHKKCRRNQI--QCKF 97
Cdd:cd20805    13 KCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGpeECDL 54
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
 46-89 2.08e-03

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. 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: 410358  Cd Length: 52  Bit Score: 36.93  E-value: 2.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2055256182  46 HSYAESKSSGLLFCNVCKKLLfslWG--AQYHECLICGIYVHKKCR 89
Cdd:cd20808     2 HNFQETTYFKPTFCDHCTGLL---WGliKQGYKCKDCGINCHKHCK 44
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 58-88 5.29e-03

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. 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: 410384  Cd Length: 61  Bit Score: 36.15  E-value: 5.29e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2055256182  58 FCNVCKKLLFSLwGAQYHECLICGIYVHKKC 88
Cdd:cd20834    20 FCSVCKEFLWGF-NKQGYQCRQCNAAVHKKC 49
PRK00106 PRK00106
ribonuclease Y;
498-638 8.04e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 39.85  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055256182 498 EEQNHITKQAKDEIVNHllplkKIKVPPEYENDSQFYQETIMKQYEKRRQRL------LSEYNDLLNKK-----SEETQI 566
Cdd:PRK00106   53 RDAEHIKKTAKRESKAL-----KKELLLEAKEEARKYREEIEQEFKSERQELkqiesrLTERATSLDRKdenlsSKEKTL 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055256182 567 HQKSQSPEDKQEDLTTSRINDKLLKMKKFQQNQREQQLIQYSYKEQLIETRRKQISSE--RELRAFQKEVQDTS 638
Cdd:PRK00106  128 ESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEiaTRIREAEREVKDRS 201
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 46-96 8.13e-03

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. 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: 410350  Cd Length: 60  Bit Score: 35.38  E-value: 8.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055256182  46 HSYAESKSSGLLFCNVCKKllfSLWGAQYH--ECLICGIYVHKKCRRN-QIQCK 96
Cdd:cd20800     5 HNWYACSHARPTYCNVCRE---ALSGVTSHglSCEVCKFKAHKRCAVKaPNNCK 55
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 58-91 9.88e-03

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of 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: 410343  Cd Length: 50  Bit Score: 34.95  E-value: 9.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2055256182  58 FCNVCKKLLFSLWgAQYHECLICGIYVHKKCRRN 91
Cdd:cd20793    13 FCDHCGSLLYGLV-RQGLKCKDCGMNVHHRCKEN 45
 
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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