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Conserved domains on  [gi|325116246|emb|CBZ51799|]
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hypothetical protein NCLIV_015910 [Neospora caninum Liverpool]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGK_acc super family cl02440
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1026-1128 6.43e-30

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.


The actual alignment was detected with superfamily member pfam00609:

Pssm-ID: 470579  Cd Length: 158  Bit Score: 116.93  E-value: 6.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  1026 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTPNIALRG-LKIFCDGEEIALPY-LEGICVV 1103
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEkVELEVDGKDLPLPKsLEGIVVL 80

                           90       100
                   ....*....|....*....|....*
gi 325116246  1104 NIPSFAGGVELWDASPESWARTSPS 1128
Cdd:pfam00609   81 NIPSYAGGTDLWGNSKEDGLGFAPQ 105
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 213-267 9.01e-23

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: 92.90  E-value: 9.01e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPLCDLG 267
Cdd:cd20805     1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGPEECDLG 55
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 815-1002 3.53e-22

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: 93.52  E-value: 3.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246    815 LVFVNVKSGGQTGKTIYKDLVGILNPLQVIDIQaEGGPTRALTFFRPLAmtKRLRVLVCGGDGTVGWIIDSIhkvygaes 894
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVP--DFNRVLVCGGDGTVGWVLNAL-------- 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246    895 leddrssegqtgedadsgdaalpistpgsetgsrgasrttdadsERHRGALRKekerakreracdlrslVPVGICPLGTG 974
Cdd:smart00046   70 --------------------------------------------DKRELPLPE----------------PPVAVLPLGTG 89

                           170       180       190
                    ....*....|....*....|....*....|..
gi 325116246    975 NDLSNVLGWGFSFDGD----IMKHLLKIQSAV 1002
Cdd:smart00046   90 NDLARSLGWGGGYDGEkllkTLRDALESDTVK 121
DAGK_acc super family cl02440
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1687-1744 1.31e-18

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.


The actual alignment was detected with superfamily member pfam00609:

Pssm-ID: 470579  Cd Length: 158  Bit Score: 84.57  E-value: 1.31e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 325116246  1687 RWRQQIINDQLIEVVGFKSLFHLGQVQVGLAKPVRICQGRDIKLILPQEIPLQIDGEP 1744
Cdd:pfam00609  101 GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
PTZ00121 super family cl31754
MAEBL; Provisional
 305-760 2.32e-09

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  305 VKEVVKEGFKEGLREMQEGVRKFNEAIVQPLKK---SLKFEQRQIAPGETGAEEPEKTPD-KKREATRRTTQLETAQDER 380
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARrqaAIKAEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAEEA 1314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  381 ETDEERSGGGERHDQDEEDTNERKTTARKVASVRKAEGEHAQTRGEATSNPDGEQRQEGTEGDRGDTALLGLGRQ----D 456
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkaD 1394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  457 ESKTRGERRRPISSLVSaiSTATEQGRSEQLASSSPGVSFAEPPTKP--EAAAPSQPSGVAREAVGLHTAGGAGEDAEST 534
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELK--KAAAAKKKADEAKKKAEEKKKADEAKKKaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  535 EEGRRC--EKGSAGESLDRGQAVGDPVEE-RRGSEPVARLRDLEDAEASWNPDSSpeNRSVETCKAWKSRSAPRKSGGCE 611
Cdd:PTZ00121 1473 DEAKKKaeEAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADE 1550

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  612 V--GLDAQEKTHRGPVSDLSSSASFSPGDGREARGSSAESAESAESAARGDAEGRGKTDHERETLAETHLKTESESDDPA 689
Cdd:PTZ00121 1551 LkkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325116246  690 GEGTLEYLREPSEAEGPTAWRAKRREEPEDTQDENEGTRQAFPRQVSEALEKGEDDSGVSGKKLRLNATRK 760
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 148-197 4.25e-07

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


The actual alignment was detected with superfamily member pfam00130:

Pssm-ID: 412127  Cd Length: 53  Bit Score: 48.21  E-value: 4.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 325116246   148 HQWEPFSSSSsPRYCSVCRQLISGFliyRNTGWACSLCQRYAHTKCLRLA 197
Cdd:pfam00130    1 HHFVHRNFKQ-PTFCDHCGEFLWGL---GKQGLKCSWCKLNVHKRCHEKV 46
 
Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1026-1128 6.43e-30

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: 116.93  E-value: 6.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  1026 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTPNIALRG-LKIFCDGEEIALPY-LEGICVV 1103
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEkVELEVDGKDLPLPKsLEGIVVL 80

                           90       100
                   ....*....|....*....|....*
gi 325116246  1104 NIPSFAGGVELWDASPESWARTSPS 1128
Cdd:pfam00609   81 NIPSYAGGTDLWGNSKEDGLGFAPQ 105
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 1026-1127 5.47e-26

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: 105.88  E-value: 5.47e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   1026 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTP--NIALRgLKIFCDGEEIALPY-LEGICV 1102
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTckDLHER-IELECDGVDVDLPNsLEGIAV 79

                            90       100
                    ....*....|....*....|....*
gi 325116246   1103 VNIPSFAGGVELWDASPESWARTSP 1127
Cdd:smart00045   80 LNIPSYGGGTNLWGTTDKEDLNFSK 104
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 213-267 9.01e-23

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: 92.90  E-value: 9.01e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPLCDLG 267
Cdd:cd20805     1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGPEECDLG 55
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 815-1002 3.53e-22

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: 93.52  E-value: 3.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246    815 LVFVNVKSGGQTGKTIYKDLVGILNPLQVIDIQaEGGPTRALTFFRPLAmtKRLRVLVCGGDGTVGWIIDSIhkvygaes 894
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVP--DFNRVLVCGGDGTVGWVLNAL-------- 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246    895 leddrssegqtgedadsgdaalpistpgsetgsrgasrttdadsERHRGALRKekerakreracdlrslVPVGICPLGTG 974
Cdd:smart00046   70 --------------------------------------------DKRELPLPE----------------PPVAVLPLGTG 89

                           170       180       190
                    ....*....|....*....|....*....|..
gi 325116246    975 NDLSNVLGWGFSFDGD----IMKHLLKIQSAV 1002
Cdd:smart00046   90 NDLARSLGWGGGYDGEkllkTLRDALESDTVK 121
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1687-1744 1.31e-18

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: 84.57  E-value: 1.31e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 325116246  1687 RWRQQIINDQLIEVVGFKSLFHLGQVQVGLAKPVRICQGRDIKLILPQEIPLQIDGEP 1744
Cdd:pfam00609  101 GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 813-1011 1.24e-17

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: 80.71  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   813 PLLVFVNVKSGGQTGKTIYKDLVGILNPLQV-IDIQAEGGPTRALTFFRPLAMTKRLRVLVCGGDGTVGWIIDSIhkvyg 891
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGL----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   892 aesleddrssegqtgedadsgdaalpistpgsetgsrgasrttdadserhrgalrkekerakreraCDLRSLVPVGICPL 971
Cdd:pfam00781   76 ------------------------------------------------------------------AGLATRPPLGIIPL 89

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 325116246   972 GTGNDLSNVLGWGfsfdGDIMKHLLKIQSAVSSTLDLWKV 1011
Cdd:pfam00781   90 GTGNDFARALGIP----GDPEEALEAILKGQTRPVDVGKV 125
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 1691-1744 3.81e-10

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: 60.43  E-value: 3.81e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 325116246   1691 QIINDQLIEVVGFKSLFHLGQVQVGLAKPVRICQGRDIKLIL--PQEIPLQIDGEP 1744
Cdd:smart00045  105 QSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIktSKTIPMQVDGEP 160
PTZ00121 PTZ00121
MAEBL; Provisional
 305-760 2.32e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  305 VKEVVKEGFKEGLREMQEGVRKFNEAIVQPLKK---SLKFEQRQIAPGETGAEEPEKTPD-KKREATRRTTQLETAQDER 380
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARrqaAIKAEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAEEA 1314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  381 ETDEERSGGGERHDQDEEDTNERKTTARKVASVRKAEGEHAQTRGEATSNPDGEQRQEGTEGDRGDTALLGLGRQ----D 456
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkaD 1394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  457 ESKTRGERRRPISSLVSaiSTATEQGRSEQLASSSPGVSFAEPPTKP--EAAAPSQPSGVAREAVGLHTAGGAGEDAEST 534
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELK--KAAAAKKKADEAKKKAEEKKKADEAKKKaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  535 EEGRRC--EKGSAGESLDRGQAVGDPVEE-RRGSEPVARLRDLEDAEASWNPDSSpeNRSVETCKAWKSRSAPRKSGGCE 611
Cdd:PTZ00121 1473 DEAKKKaeEAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADE 1550

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  612 V--GLDAQEKTHRGPVSDLSSSASFSPGDGREARGSSAESAESAESAARGDAEGRGKTDHERETLAETHLKTESESDDPA 689
Cdd:PTZ00121 1551 LkkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325116246  690 GEGTLEYLREPSEAEGPTAWRAKRREEPEDTQDENEGTRQAFPRQVSEALEKGEDDSGVSGKKLRLNATRK 760
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 213-267 4.20e-08

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


Pssm-ID: 395079  Cd Length: 53  Bit Score: 51.29  E-value: 4.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 325116246   213 HVFVQGNLSADATCCCCGLACSSnFGLDGLRCLWCNRTLHEECRHRLPsPLCDLG 267
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWG-LGKQGLKCSWCKLNVHKRCHEKVP-PECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 148-197 4.25e-07

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: 48.21  E-value: 4.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 325116246   148 HQWEPFSSSSsPRYCSVCRQLISGFliyRNTGWACSLCQRYAHTKCLRLA 197
Cdd:pfam00130    1 HHFVHRNFKQ-PTFCDHCGEFLWGL---GKQGLKCSWCKLNVHKRCHEKV 46
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 148-197 6.35e-07

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: 47.90  E-value: 6.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 325116246  148 HQWEPFSSSSsPRYCSVCRQLISGFLiyrNTGWACSLCQRYAHTKCLRLA 197
Cdd:cd00029     1 HRFVPTTFSS-PTFCDVCGKLIWGLF---KQGLKCSDCGLVCHKKCLDKA 46
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 148-197 2.85e-05

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: 43.23  E-value: 2.85e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 325116246    148 HQWEpFSSSSSPRYCSVCRQLISGfliYRNTGWACSLCQRYAHTKCLRLA 197
Cdd:smart00109    1 HKHV-FRTFTKPTFCCVCRKSIWG---SFKQGLRCSECKVKCHKKCADKV 46
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 964-1119 1.08e-04

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 46.38  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  964 VPVGICPLGTGNDLSNVLGwgfsFDGDIMKHLLKIQSAVSSTLDLWKVkvtsdktNATLvettFSNYLDVGVAARIVLKF 1043
Cdd:COG1597    83 PPLGILPLGTGNDFARALG----IPLDPEAALEALLTGRTRRIDLGRV-------NGRY----FLNVAGIGFDAEVVERA 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325116246 1044 HKLReenpelfQSRLGnKFLYGEVGFRDFLVTPNIALRglkIFCDGEEIALPYLeGICVVNIPSFAGGVEL-WDASP 1119
Cdd:COG1597   148 NRAL-------KRRLG-KLAYVLAALRALLRYRPFRLR---IELDGEEIEGEAL-LVAVGNGPYYGGGLRLaPDASL 212
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 213-262 1.32e-03

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: 38.22  E-value: 1.32e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 325116246    213 HVFVQGNLSADATCCCCGLACSSNFgLDGLRCLWCNRTLHEECRHRLPSP 262
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSF-KQGLRCSECKVKCHKKCADKVPKA 49
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 355-562 5.40e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 5.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   355 EPEKTPDKKREATRRTTQLETAQDERETDEERSGGGERHDQDEEDTNERKTTAR-KVASVRKAEGEHAQTRGEATSNP-- 431
Cdd:TIGR00927  637 EAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKgEQEGEGEIEAKEADHKGETEAEEve 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   432 -DGEQRQEGTEgDRGDTALLGLGRQDESKTRGERRRPisslvSAISTATEQGRSEQLASSSPGVSFAEPPTKPEAaapsq 510
Cdd:TIGR00927  717 hEGETEAEGTE-DEGEIETGEEGEEVEDEGEGEAEGK-----HEVETEGDRKETEHEGETEAEGKEDEDEGEIQA----- 785

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 325116246   511 psGVAREAVGLHTAGGAGEDAESTEEGRRCEKGSAGESLDRGQAVGDPVEER 562
Cdd:TIGR00927  786 --GEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQ 835
 
Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1026-1128 6.43e-30

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: 116.93  E-value: 6.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  1026 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTPNIALRG-LKIFCDGEEIALPY-LEGICVV 1103
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEkVELEVDGKDLPLPKsLEGIVVL 80

                           90       100
                   ....*....|....*....|....*
gi 325116246  1104 NIPSFAGGVELWDASPESWARTSPS 1128
Cdd:pfam00609   81 NIPSYAGGTDLWGNSKEDGLGFAPQ 105
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 1026-1127 5.47e-26

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: 105.88  E-value: 5.47e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   1026 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTP--NIALRgLKIFCDGEEIALPY-LEGICV 1102
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTckDLHER-IELECDGVDVDLPNsLEGIAV 79

                            90       100
                    ....*....|....*....|....*
gi 325116246   1103 VNIPSFAGGVELWDASPESWARTSP 1127
Cdd:smart00045   80 LNIPSYGGGTNLWGTTDKEDLNFSK 104
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 213-267 9.01e-23

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: 92.90  E-value: 9.01e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPLCDLG 267
Cdd:cd20805     1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGPEECDLG 55
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 815-1002 3.53e-22

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: 93.52  E-value: 3.53e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246    815 LVFVNVKSGGQTGKTIYKDLVGILNPLQVIDIQaEGGPTRALTFFRPLAmtKRLRVLVCGGDGTVGWIIDSIhkvygaes 894
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVP--DFNRVLVCGGDGTVGWVLNAL-------- 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246    895 leddrssegqtgedadsgdaalpistpgsetgsrgasrttdadsERHRGALRKekerakreracdlrslVPVGICPLGTG 974
Cdd:smart00046   70 --------------------------------------------DKRELPLPE----------------PPVAVLPLGTG 89

                           170       180       190
                    ....*....|....*....|....*....|..
gi 325116246    975 NDLSNVLGWGFSFDGD----IMKHLLKIQSAV 1002
Cdd:smart00046   90 NDLARSLGWGGGYDGEkllkTLRDALESDTVK 121
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 213-276 5.09e-19

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: 82.33  E-value: 5.09e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSpLCDLGPFRQLILPP 276
Cdd:cd20853     1 HHWVRGNLPLCSVCCVCNEQCGNQPGLCDYRCCWCQRTVHDDCLAKLPK-ECDLGAFRNFIVPP 63
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1687-1744 1.31e-18

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: 84.57  E-value: 1.31e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 325116246  1687 RWRQQIINDQLIEVVGFKSLFHLGQVQVGLAKPVRICQGRDIKLILPQEIPLQIDGEP 1744
Cdd:pfam00609  101 GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 813-1011 1.24e-17

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: 80.71  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   813 PLLVFVNVKSGGQTGKTIYKDLVGILNPLQV-IDIQAEGGPTRALTFFRPLAMTKRLRVLVCGGDGTVGWIIDSIhkvyg 891
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGL----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   892 aesleddrssegqtgedadsgdaalpistpgsetgsrgasrttdadserhrgalrkekerakreraCDLRSLVPVGICPL 971
Cdd:pfam00781   76 ------------------------------------------------------------------AGLATRPPLGIIPL 89

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 325116246   972 GTGNDLSNVLGWGfsfdGDIMKHLLKIQSAVSSTLDLWKV 1011
Cdd:pfam00781   90 GTGNDFARALGIP----GDPEEALEAILKGQTRPVDVGKV 125
C1_DGKtheta_typeV_rpt3 cd20854
third protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 213-276 1.30e-10

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: 58.43  E-value: 1.30e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPsPLCDLGPFRQLILPP 276
Cdd:cd20854     1 HHWREGNLPSNSKCEVCKKSCGSSECLAGMRCEWCGITAHASCYKSLP-KECNFGRLRNIILPP 63
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 1691-1744 3.81e-10

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: 60.43  E-value: 3.81e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 325116246   1691 QIINDQLIEVVGFKSLFHLGQVQVGLAKPVRICQGRDIKLIL--PQEIPLQIDGEP 1744
Cdd:smart00045  105 QSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIktSKTIPMQVDGEP 160
PTZ00121 PTZ00121
MAEBL; Provisional
 305-760 2.32e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  305 VKEVVKEGFKEGLREMQEGVRKFNEAIVQPLKK---SLKFEQRQIAPGETGAEEPEKTPD-KKREATRRTTQLETAQDER 380
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARrqaAIKAEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAEEA 1314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  381 ETDEERSGGGERHDQDEEDTNERKTTARKVASVRKAEGEHAQTRGEATSNPDGEQRQEGTEGDRGDTALLGLGRQ----D 456
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkaD 1394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  457 ESKTRGERRRPISSLVSaiSTATEQGRSEQLASSSPGVSFAEPPTKP--EAAAPSQPSGVAREAVGLHTAGGAGEDAEST 534
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELK--KAAAAKKKADEAKKKAEEKKKADEAKKKaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  535 EEGRRC--EKGSAGESLDRGQAVGDPVEE-RRGSEPVARLRDLEDAEASWNPDSSpeNRSVETCKAWKSRSAPRKSGGCE 611
Cdd:PTZ00121 1473 DEAKKKaeEAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADE 1550

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  612 V--GLDAQEKTHRGPVSDLSSSASFSPGDGREARGSSAESAESAESAARGDAEGRGKTDHERETLAETHLKTESESDDPA 689
Cdd:PTZ00121 1551 LkkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325116246  690 GEGTLEYLREPSEAEGPTAWRAKRREEPEDTQDENEGTRQAFPRQVSEALEKGEDDSGVSGKKLRLNATRK 760
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
C1_DGKalpha_rpt2 cd20890
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha ...
 213-276 2.85e-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: 54.85  E-value: 2.85e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325116246  213 HVFVQGNLSAdATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPlCDLGPFRQLILPP 276
Cdd:cd20890     1 HVWVSGGCES-SKCDKCQKKIKSFQSLTGLHCVWCHLKRHDECLSSVPST-CDCGPLRDHILPP 62
C1_DGK_typeII_rpt2 cd20852
second protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 213-267 4.60e-09

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: 53.87  E-value: 4.60e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPlCDLG 267
Cdd:cd20852     1 HQWLEGNLPVSSKCAVCDKTCGSVLRLQDWRCLWCGATVHTACKDSLPTK-CSLG 54
C1_DGKdelta_rpt2 cd20893
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
 212-267 6.06e-09

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: 53.91  E-value: 6.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 325116246  212 PHVFVQGNLSADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPlCDLG 267
Cdd:cd20893     5 PHQWLEGNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKELLLTK-CPLG 59
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 213-267 4.20e-08

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


Pssm-ID: 395079  Cd Length: 53  Bit Score: 51.29  E-value: 4.20e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 325116246   213 HVFVQGNLSADATCCCCGLACSSnFGLDGLRCLWCNRTLHEECRHRLPsPLCDLG 267
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWG-LGKQGLKCSWCKLNVHKRCHEKVP-PECGCD 53
PTZ00121 PTZ00121
MAEBL; Provisional
 315-760 9.55e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 9.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  315 EGLREMQEGVRKFNEAIVQPLKKSLKFEQRQIAPGETGAEEPEKTPDKKREATRRTTQLETAQDE-RETDEERSGGGERH 393
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAaKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  394 DQDEEDTNERKTTARKVASVRKAE-----------GEHAQTRGEATSNPDgEQRQEGTEGDRGDTALLGL---GRQDESK 459
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADeakkkaeekkkADEAKKKAEEAKKAD-EAKKKAEEAKKAEEAKKKAeeaKKADEAK 1476

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  460 TRGERRRPISSLVSAISTATEqgRSEQLASSSPGVSFAEPPTKPEAAAPSQPSGVAREAvglhtagGAGEDAESTEEGRR 539
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA-------KKADEAKKAEEKKK 1547

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  540 CEKGSAGESLDRGQAVGDPVEERRGSE----PVARLRDLEDAEASWNPDSSPENRSVETCKAWKSRSAPRKSGGCEVGLD 615
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEdknmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  616 AQEKthRGPVSDLSSSASFSPGDGREARGSSAESAESAESAARGDAEGRGKTDHERETLAETHLKTESESDDPAGEGTLE 695
Cdd:PTZ00121 1628 AEEE--KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 325116246  696 YLREPSEAEgptawrAKRREEPEDTQDENEGTRQAFPRQVSEALEKGEDDSGVSGKKLRLNATRK 760
Cdd:PTZ00121 1706 ELKKKEAEE------KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
C1_DGKeta_rpt2 cd20894
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 212-270 1.81e-07

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: 49.51  E-value: 1.81e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 325116246  212 PHVFVQGNLSADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPsPLCDLGPFR 270
Cdd:cd20894     5 PHQWLEGNLPVSAKCSVCDKTCGSVLRLQDWRCLWCKAMVHTACKDQYP-RKCPLGQCR 62
C1_DGK_typeI_like_rpt2 cd20851
second protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 213-267 1.83e-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: 49.27  E-value: 1.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 325116246  213 HVFVQGNlsADATCCCCGLACSSNFGLDGLRCLWCNRTLHEECrHRLPSPLCDLG 267
Cdd:cd20851     1 HHWVEGN--CPGKCDKCHKSIKSYQGLTGLHCVWCHITLHNKC-ASHVKPECDLG 52
C1_DGKbeta_rpt2 cd20891
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta ...
 213-270 4.05e-07

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: 48.44  E-value: 4.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSnfGLDGLRCLWCNRTLHEECRHRLpSPLCDLGPFR 270
Cdd:cd20891     3 HFWVEGNCPTKCDKCHKTIKCYQ--GLTGLHCVWCQITLHNKCASHV-KPECDCGPLK 57
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 148-197 4.25e-07

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: 48.21  E-value: 4.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 325116246   148 HQWEPFSSSSsPRYCSVCRQLISGFliyRNTGWACSLCQRYAHTKCLRLA 197
Cdd:pfam00130    1 HHFVHRNFKQ-PTFCDHCGEFLWGL---GKQGLKCSWCKLNVHKRCHEKV 46
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 148-197 6.35e-07

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: 47.90  E-value: 6.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 325116246  148 HQWEPFSSSSsPRYCSVCRQLISGFLiyrNTGWACSLCQRYAHTKCLRLA 197
Cdd:cd00029     1 HRFVPTTFSS-PTFCDVCGKLIWGLF---KQGLKCSDCGLVCHKKCLDKA 46
C1_DGKgamma_rpt2 cd20892
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
 213-276 1.13e-06

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: 47.50  E-value: 1.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSnfGLDGLRCLWCNRTLHEECrHRLPSPLCDLGPFRQLILPP 276
Cdd:cd20892     1 HVWVEGNSPVKCDRCHKSIKCYQ--GLTGLHCVWCQITLHNKC-ASHVSPECDGGQLKDHILLP 61
PTZ00121 PTZ00121
MAEBL; Provisional
 340-744 3.14e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  340 KFEQ-RQIAPGETGAEEPEKTPDKKREATRRTTQLETAQDERETDEERsgggeRHDQDEEDTNERKTT-ARKVASVRKAE 417
Cdd:PTZ00121 1099 KAEEaKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-----KAEDAKRVEIARKAEdARKAEEARKAE 1173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  418 -GEHAQTRGEATSNPDGEQRQEGTEGDRGDTAllglgRQDESKTRGE--RRRPISSLVSAISTATEQGRSEQLASSSPGV 494
Cdd:PTZ00121 1174 dAKKAEAARKAEEVRKAEELRKAEDARKAEAA-----RKAEEERKAEeaRKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE 1248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  495 SFAEPPTKPEAAAPSQPSgvAREAVGLHTAGGAGEDAESTEEGRRCEKGSAGESLDRGQAVGDPVEERRGSEPVARLRDL 574
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFA--RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  575 EDAEASWNPDSSPENRSVETCKAWKSRSAPRKSGGCEVGLDAQEKTHrgpvsdlsssasfspgdgREARGSSAESAESAE 654
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK------------------EEAKKKADAAKKKAE 1388

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  655 SAARGDaEGRGKTDHERETLAETHLKTESESDDPAGEGTLEYLREPSEA-----EGPTAWRAKRREEpEDTQDENEGTRQ 729
Cdd:PTZ00121 1389 EKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAkkkaeEAKKADEAKKKAE-EAKKAEEAKKKA 1466

                         410
                  ....*....|....*
gi 325116246  730 AFPRQVSEALEKGED 744
Cdd:PTZ00121 1467 EEAKKADEAKKKAEE 1481
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 161-202 1.52e-05

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


Pssm-ID: 410355  Cd Length: 55  Bit Score: 43.98  E-value: 1.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 325116246  161 YCSVCRQLISGflIYRNTGWACSLCQRYAHTKCLRLAERLDC 202
Cdd:cd20805    13 KCSVCGKKCGS--SFGLAGYRCSWCKRTVHSECIDKLGPEEC 52
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 213-262 2.37e-05

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: 43.27  E-value: 2.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 325116246  213 HVFVQGNLSADATCCCCGLACSSnFGLDGLRCLWCNRTLHEECRHRLPSP 262
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWG-LFKQGLKCSDCGLVCHKKCLDKAPSP 49
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 148-197 2.85e-05

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: 43.23  E-value: 2.85e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 325116246    148 HQWEpFSSSSSPRYCSVCRQLISGfliYRNTGWACSLCQRYAHTKCLRLA 197
Cdd:smart00109    1 HKHV-FRTFTKPTFCCVCRKSIWG---SFKQGLRCSECKVKCHKKCADKV 46
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 342-466 4.66e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 48.36  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  342 EQRQIAPGETGAEEPEKTPDKKREATRRTTQLETAQDERETDEERSGGGERHDQDEEDTNERKTTARKVASVRKAEGEHA 421
Cdd:PRK12678  100 AKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDRE 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 325116246  422 QTRGEATSnpdGEQRQEGTEGDRGDTALLGLGRQDESKTRGERRR 466
Cdd:PRK12678  180 DRQAEAER---GERGRREERGRDGDDRDRRDRREQGDRREERGRR 221
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 964-1119 1.08e-04

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 46.38  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  964 VPVGICPLGTGNDLSNVLGwgfsFDGDIMKHLLKIQSAVSSTLDLWKVkvtsdktNATLvettFSNYLDVGVAARIVLKF 1043
Cdd:COG1597    83 PPLGILPLGTGNDFARALG----IPLDPEAALEALLTGRTRRIDLGRV-------NGRY----FLNVAGIGFDAEVVERA 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325116246 1044 HKLReenpelfQSRLGnKFLYGEVGFRDFLVTPNIALRglkIFCDGEEIALPYLeGICVVNIPSFAGGVEL-WDASP 1119
Cdd:COG1597   148 NRAL-------KRRLG-KLAYVLAALRALLRYRPFRLR---IELDGEEIEGEAL-LVAVGNGPYYGGGLRLaPDASL 212
PTZ00121 PTZ00121
MAEBL; Provisional
 315-792 1.31e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  315 EGLREMQEGvRKFNEAivQPLKKSLKFEQRQIAPGETGAEEPEKTPDKKR-EATRRTTQLETAQDERETDEERSGGGERH 393
Cdd:PTZ00121 1161 EDARKAEEA-RKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKKAEEAKK 1237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  394 DQDEEDTNERKTTARKVASVRKAEGEHAQTRGEATSNPDGEQRQEGTEGDRGDTAllglgrqDESKTRGERRRpissLVS 473
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA-------DEAKKAEEKKK----ADE 1306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  474 AISTATEQGRSEQLASSSpgvsfAEPPTKPEAAAPSQPSGVAREAVGLHTAGGAGEDAESTEEGRRCEKGSAGESLDRGQ 553
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKA-----EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  554 AVGDPVEERRGSEPVARLRDLEDAEASWNPDSSPENRSVETCKawksRSAPRKSGGCEVGLDAQEKTHRGPVSDLSSSAS 633
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK----KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  634 FSPGDGREARGSSAESAESAESAARGDAEGRGKTDHERETLAEtHLKTESESDDPAGEgtleyLREPSEAEgpTAWRAKR 713
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADE-----AKKAEEAK--KADEAKK 1529

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  714 REEPEDTQD--ENEGTRQAFPRQVSEALEKGEDDSGVSGKKlrlNATRKVGMPPGTGSKARRKDSSRTQMMYSVAKAMPP 791
Cdd:PTZ00121 1530 AEEAKKADEakKAEEKKKADELKKAEELKKAEEKKKAEEAK---KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606


                  .
gi 325116246  792 M 792
Cdd:PTZ00121 1607 M 1607
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 145-203 1.64e-04

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: 41.15  E-value: 1.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325116246  145 KSLHQWEPFSSSSSPRYCSVCRQLI-SGFLiyrntgwaCSLCQRYAHTKCLRLAER-LDCK 203
Cdd:cd20801     1 SKGHHWVSTDLFSKPTYCSVCETLIlSGAF--------CDCCGLCVDEGCLRKADKrFPCK 53
PTZ00121 PTZ00121
MAEBL; Provisional
 363-780 8.15e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 8.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  363 KREATRRTTQLETAQDERETDEERSGGGERHDQDEEDTNERKTTARKVASVRKAE----GEHAQtRGEATSNPDGEQRQE 438
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEAR-KAEDAKRVEIARKAE 1161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  439 gtEGDRGDTALlglgRQDESKTRGERRRPISSLVSAISTATEQGRSEQLASSSPGVSFAEPPTKPEAAAPSQPSGVAREA 518
Cdd:PTZ00121 1162 --DARKAEEAR----KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEA 1235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  519 VGLHTAGGAGEDAESTEEGRRCEKGSAGESLDRGQAVgdPVEERRGSEPVARLRDLEDAEASwnpDSSPENRSVETCKaw 598
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI--KAEEARKADELKKAEEKKKADEA---KKAEEKKKADEAK-- 1308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  599 ksRSAPRKSGGCEVGLDAQEKTHRGPVSDLSSSASFSPGDGREARGSSAESAESAESAARGDAEgrGKTDHERETLAEth 678
Cdd:PTZ00121 1309 --KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAKKKADA-- 1382

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  679 LKTESESDDPAGEgtleyLREPSEAEGPTAWRAKRREEPEDTQDENEGTRQAfPRQVSEALEKGEDDSGVSGKKLRLNAT 758
Cdd:PTZ00121 1383 AKKKAEEKKKADE-----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEA 1456

                         410       420
                  ....*....|....*....|..
gi 325116246  759 RKVGMPPGTGSKARRKDSSRTQ 780
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKK 1478
PTZ00121 PTZ00121
MAEBL; Provisional
 315-743 1.16e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  315 EGLREMQEGVRKFNEAIVQPLKKSLKFEQ-RQIAPGETGAEEPEKTPDKKREATRRTTQLETAQ--DERETDEERSGGGE 391
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKAE 1460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  392 RHDQDEEDTNERKTTARKVASVRKAEgeHAQTRGEATSNPDGEQRQEGTEGDRGDTAllglgRQDESKTRGERRRPISSL 471
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAAEAKKKADEA-----KKAEEAKKADEAKKAEEA 1533

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  472 VSA--ISTATEQGRSEQLASSSPgVSFAEPPTKPEAAAPSQpsgvAREAVGLHTAggagEDAESTEEGRRCE--KGSAGE 547
Cdd:PTZ00121 1534 KKAdeAKKAEEKKKADELKKAEE-LKKAEEKKKAEEAKKAE----EDKNMALRKA----EEAKKAEEARIEEvmKLYEEE 1604

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  548 SLDRGQAVGDPVEERRGSEPVARLRDLEDAEASWNPDSSPENRSVETCKAWKSRSAPRKSGGCEVGLDAQEKTHRGPVSD 627
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  628 LSSSASFSPGDGREARGSSAESAESAESAARGDAEGRGKTDHERETLAEtHLKTESESDDPAGE---------GTLEYLR 698
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKKKAEeakkdeeekKKIAHLK 1763

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 325116246  699 EPSEAEGPTAWRAKRREEPEDTQDENEGTRQAFPRQVSEALEKGE 743
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 148-197 1.29e-03

first 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 first 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: 410349  Cd Length: 62  Bit Score: 38.89  E-value: 1.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 325116246  148 HQWEPfSSSSSPRYCSVCRQLISGFliyRNTGWACSLCQRYAHTKCLRLA 197
Cdd:cd20799     6 HVWRL-KHFNKPAYCNVCENMLVGL---RKQGLCCTFCKYTVHERCVSRA 51
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 213-262 1.32e-03

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: 38.22  E-value: 1.32e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 325116246    213 HVFVQGNLSADATCCCCGLACSSNFgLDGLRCLWCNRTLHEECRHRLPSP 262
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSF-KQGLRCSECKVKCHKKCADKVPKA 49
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 130-193 1.41e-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: 38.46  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325116246  130 RVHHYNkagSHGLIPKSLHQwepfsssssPRYCSVCRQLISGFliyRNTGWACSLCQRYAHTKC 193
Cdd:cd20834     1 KVHEVK---GHEFIAKFFRQ---------PTFCSVCKEFLWGF---NKQGYQCRQCNAAVHKKC 49
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
 159-203 2.52e-03

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: 37.62  E-value: 2.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 325116246  159 PRYCSVCRQLISGfLIYRntGWACSLCQRYAHTKCLRLAERldCK 203
Cdd:cd20810    13 PTTCSVCKKLLKG-LFFQ--GYKCSVCGAAVHKECIAKVKR--CG 52
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 342-466 3.65e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  342 EQRQIAPGETGAEEPEKTPDKKREATRRTTQLETAQDERETDEERSGGGERHDQDEEDTNERKTTARKvasvrkAEGEHA 421
Cdd:PRK12678  151 QPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREER------GRRDGG 224

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 325116246  422 QTRGEATSNPDGEQRQEGTEGDRGDtallglGRQDESKTRGERRR 466
Cdd:PRK12678  225 DRRGRRRRRDRRDARGDDNREDRGD------RDGDDGEGRGGRRG 263
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 355-562 5.40e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 5.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   355 EPEKTPDKKREATRRTTQLETAQDERETDEERSGGGERHDQDEEDTNERKTTAR-KVASVRKAEGEHAQTRGEATSNP-- 431
Cdd:TIGR00927  637 EAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKgEQEGEGEIEAKEADHKGETEAEEve 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246   432 -DGEQRQEGTEgDRGDTALLGLGRQDESKTRGERRRPisslvSAISTATEQGRSEQLASSSPGVSFAEPPTKPEAaapsq 510
Cdd:TIGR00927  717 hEGETEAEGTE-DEGEIETGEEGEEVEDEGEGEAEGK-----HEVETEGDRKETEHEGETEAEGKEDEDEGEIQA----- 785

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 325116246   511 psGVAREAVGLHTAGGAGEDAESTEEGRRCEKGSAGESLDRGQAVGDPVEER 562
Cdd:TIGR00927  786 --GEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQ 835
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 128-193 5.87e-03

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: 37.06  E-value: 5.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 325116246  128 RYRVHHYNkagSHGLIPKSLHQwepfsssssPRYCSVCRQLISGflIYRNTGWACSLCQRYAHTKC 193
Cdd:cd20835     1 RRRVHQVN---GHKFMATYLRQ---------PTYCSHCKDFIWG--VIGKQGYQCQVCTCVVHKRC 52
PHA03169 PHA03169
hypothetical protein; Provisional
 392-588 7.78e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  392 RHDQDEEDTNERKTTARKVASVRK----AEGEHAQTRGEATSNPDGEQRQE------GTEGDRGDTALLGLGRQDESKTR 461
Cdd:PHA03169   25 RHGGTREQAGRRRGTAARAAKPAPpaptTSGPQVRAVAEQGHRQTESDTETaeesrhGEKEERGQGGPSGSGSESVGSPT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  462 GERRRPISSLVSAIS-TATEQGRSEQLASSSPGvsfAEPPTKPEAAAPSQPSgvarEAVGLHTAGGAGEDAESTEEGRrc 540
Cdd:PHA03169  105 PSPSGSAEELASGLSpENTSGSSPESPASHSPP---PSPPSHPGPHEPAPPE----SHNPSPNQQPSSFLQPSHEDSP-- 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 325116246  541 EKGSAGESLDRGQAVGDP-VEERRGSEPVARLRDLEDAEASWNPDSSPE 588
Cdd:PHA03169  176 EEPEPPTSEPEPDSPGPPqSETPTSSPPPQSPPDEPGEPQSPTPQQAPS 224
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 370-537 8.41e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 40.73  E-value: 8.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  370 TTQLETAQDERETDEERSGGGERHDQDeedtnerKTTARKVASVRKAEGEHAQTRGEATSNPDGEQRQEGTEGDRGDTAl 449
Cdd:PRK13108  301 AELAAAAVASAASAVGPVGPGEPNQPD-------DVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIE- 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325116246  450 lglgRQDESKTRGERrrpisslvsaistATEQGRSEQLASSSPGVSFAEPPTKPEAAAPSQPSGVAREAvglhtagGAGE 529
Cdd:PRK13108  373 ----REQPGDLAGQA-------------PAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIP-------DPAK 428


                  ....*...
gi 325116246  530 DAESTEEG 537
Cdd:PRK13108  429 PDELAVAG 436
 
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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