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Conserved domains on  [gi|1379059808|gb|PUA87047|]
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putative diacylglycerol kinase [Toxoplasma gondii TgCATBr9]

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 ...
 1007-1109 8.58e-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: 116.55  E-value: 8.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1007 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTPNIALRG-LKIFCDGQEIALPY-LEGICVV 1084
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEkVELEVDGKDLPLPKsLEGIVVL 80

                           90       100
                   ....*....|....*....|....*
gi 1379059808 1085 NIPSFAGGVELWDTAPESWAASASP 1109
Cdd:pfam00609   81 NIPSYAGGTDLWGNSKEDGLGFAPQ 105
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 223-277 1.30e-22

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: 92.51  E-value: 1.30e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPLCDLG 277
Cdd:cd20805      1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGPEECDLG 55
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 811-983 2.61e-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: 93.90  E-value: 2.61e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808   811 LVFVNVKSGGQTGKAIYKDLVAILNPLQVIDIQaEGGPSRALSFFRPLAmtKRLRVLVCGGDGTVGWIIDSIhkvygaea 890
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVP--DFNRVLVCGGDGTVGWVLNAL-------- 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808   891 aeeergseAQTGDEVDSgeaagkvgvesegrrgrresegvawgsrdracdlrslVPVGICPLGTGNDLSNVLGWGFSFDG 970
Cdd:smart00046   70 --------DKRELPLPE-------------------------------------PPVAVLPLGTGNDLARSLGWGGGYDG 104

                           170
                    ....*....|....*..
gi 1379059808   971 D----IMKHLLKIQSAV 983
Cdd:smart00046  105 EkllkTLRDALESDTVK 121
DAGK_acc super family cl02440
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1703-1760 2.30e-17

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: 81.11  E-value: 2.30e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1379059808 1703 RWRQQIINDQLIEVVGFKSLFHLGQVQVGLAKPVRLCQGRDIQLVLPQEIPLQIDGEP 1760
Cdd:pfam00609  101 GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 158-207 5.91e-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: 47.82  E-value: 5.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1379059808  158 HQWEPFSSSSsPRYCSVCRQLISGFliyRNTGWACTLCQRYAHTKCLRLA 207
Cdd:pfam00130    1 HHFVHRNFKQ-PTFCDHCGEFLWGL---GKQGLKCSWCKLNVHKRCHEKV 46
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 356-485 1.32e-05

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


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 50.38  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  356 VQGERGKTRLEGAHEKQREgkGDAHQLASEVEENRSTEQASGEAECRGNSGGSREAESGEDPL--ANEATRESKSVENES 433
Cdd:TIGR00927  740 EVEDEGEGEAEGKHEVETE--GDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKveHEGETEAGEKDEHEG 817

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1379059808  434 VDKEKEKDAQKKPREETCELVGEEEQEDAtrgdgSDNPPVDPGGKKDGGRSE 485
Cdd:TIGR00927  818 QSETQADDTEVKDETGEQELNAENQGEAK-----QDEKGVDGGGGSDGGDSE 864
MDN1 super family cl34967
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 381-742 1.23e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5271:

Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 47.32  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  381 QLASEVEENRSTEQASGEAECRGNSGGSREAESGEDPLANEATREsksvENESVDKEKEKDAQKKPREETCELVGEEEQE 460
Cdd:COG5271    423 DASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEE----DTESAEEDADGDEATDEDDASDDGDEEEAEE 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  461 DATRGDGSDNPPV-----DPGGKKDgGRSEPPRILSRFSESKGQPKPTTTARDSSTDSAAPSLTAASSDTQRLPEAEQTQ 535
Cdd:COG5271    499 DAEAEADSDELTAeetsaDDGADTD-AAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETED 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  536 DARSQRTDaspwgenKSTGGGQAGEAVEQHGDSAAIERGTGDREAAETSQPhgwAPDSSGETlHTPARDDPPCPHNARRK 615
Cdd:COG5271    578 ATENADAD-------ETEESADESEEAEASEDEAAEEEEADDDEADADADG---AADEEETE-EEAAEDEAAEPETDASE 646

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  616 LASTQRDEKQREGTAcllASAASsfachgppEPLGSHRPTAGAATSEEGDE-SRCQKTESENDGLGSGDVVRVGGFTDFT 694
Cdd:COG5271    647 AADEDADAETEAEAS---ADESE--------EEAEDESETSSEDAEEDADAaAAEASDDEEETEEADEDAETASEEADAE 715

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1379059808  695 EERSEEDLRTPSLEK---GSEGQDARQTEPDGRQKSGAPSEEALEKEDASV 742
Cdd:COG5271    716 EADTEADGTAEEAEEaaeEAESADEEAASLPDEADAEEEAEEAEEAEEDDA 766
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 1365-1544 5.04e-03

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.81  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1365 EPAVELRGASPTDAGSRRRCVSEESREKRRLERTPVPDAGDRHEGDRGNlPSGSKASRSTADPEIAPAVAPQELSPKDSD 1444
Cdd:PRK12678   104 AAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQP-ATEARADAAERTEEEERDERRRRGDREDRQ 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1445 -GCTRDRQKKSQSKAAEEDDDSVDRPFAGSSQRKSRVScstsplKNRKTKDSHNRKRSARGAGRGVWHTRGQSLEDVSVS 1523
Cdd:PRK12678   183 aEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR------RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256

                          170       180
                   ....*....|....*....|.
gi 1379059808 1524 ELSPRRARRGRNVEERLRKGR 1544
Cdd:PRK12678   257 GRGGRRGRRFRDRDRRGRRGG 277
 
Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1007-1109 8.58e-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: 116.55  E-value: 8.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1007 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTPNIALRG-LKIFCDGQEIALPY-LEGICVV 1084
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEkVELEVDGKDLPLPKsLEGIVVL 80

                           90       100
                   ....*....|....*....|....*
gi 1379059808 1085 NIPSFAGGVELWDTAPESWAASASP 1109
Cdd:pfam00609   81 NIPSYAGGTDLWGNSKEDGLGFAPQ 105
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 1007-1102 4.42e-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: 106.27  E-value: 4.42e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  1007 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTP--NIALRgLKIFCDGQEIALPY-LEGICV 1083
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTckDLHER-IELECDGVDVDLPNsLEGIAV 79

                            90
                    ....*....|....*....
gi 1379059808  1084 VNIPSFAGGVELWDTAPES 1102
Cdd:smart00045   80 LNIPSYGGGTNLWGTTDKE 98
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 223-277 1.30e-22

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: 92.51  E-value: 1.30e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPLCDLG 277
Cdd:cd20805      1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGPEECDLG 55
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 811-983 2.61e-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: 93.90  E-value: 2.61e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808   811 LVFVNVKSGGQTGKAIYKDLVAILNPLQVIDIQaEGGPSRALSFFRPLAmtKRLRVLVCGGDGTVGWIIDSIhkvygaea 890
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVP--DFNRVLVCGGDGTVGWVLNAL-------- 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808   891 aeeergseAQTGDEVDSgeaagkvgvesegrrgrresegvawgsrdracdlrslVPVGICPLGTGNDLSNVLGWGFSFDG 970
Cdd:smart00046   70 --------DKRELPLPE-------------------------------------PPVAVLPLGTGNDLARSLGWGGGYDG 104

                           170
                    ....*....|....*..
gi 1379059808   971 D----IMKHLLKIQSAV 983
Cdd:smart00046  105 EkllkTLRDALESDTVK 121
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 809-992 6.77e-20

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: 87.26  E-value: 6.77e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  809 PLLVFVNVKSGGQTGKAIYKDLVAILNPLQV-IDIQAEGGPSRALSFFRPLAMTKRLRVLVCGGDGTVGWIIDsihkvyg 887
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLN------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  888 aeaaeeergseaqtgdevdsgeaagkvgvesegrrgrreseGVAWGSRDracdlrslVPVGICPLGTGNDLSNVLGWGfs 967
Cdd:pfam00781   74 -----------------------------------------GLAGLATR--------PPLGIIPLGTGNDFARALGIP-- 102

                          170       180
                   ....*....|....*....|....*
gi 1379059808  968 fdGDIMKHLLKIQSAVSSTLDLWKV 992
Cdd:pfam00781  103 --GDPEEALEAILKGQTRPVDVGKV 125
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1703-1760 2.30e-17

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: 81.11  E-value: 2.30e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1379059808 1703 RWRQQIINDQLIEVVGFKSLFHLGQVQVGLAKPVRLCQGRDIQLVLPQEIPLQIDGEP 1760
Cdd:pfam00609  101 GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 1707-1760 1.80e-09

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: 58.50  E-value: 1.80e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1379059808  1707 QIINDQLIEVVGFKSLFHLGQVQVGLAKPVRLCQGRDIQLVL--PQEIPLQIDGEP 1760
Cdd:smart00045  105 QSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIktSKTIPMQVDGEP 160
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 223-277 1.93e-08

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


Pssm-ID: 395079  Cd Length: 53  Bit Score: 52.06  E-value: 1.93e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSnFGLDGLRCLWCNRTLHEECRHRLPsPLCDLG 277
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWG-LGKQGLKCSWCKLNVHKRCHEKVP-PECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 158-207 5.91e-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: 47.82  E-value: 5.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1379059808  158 HQWEPFSSSSsPRYCSVCRQLISGFliyRNTGWACTLCQRYAHTKCLRLA 207
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 ...
 158-212 6.21e-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: 6.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  158 HQWEPFSSSSsPRYCSVCRQLISGFLiyrNTGWACTLCQRYAHTKCLRLAERlDC 212
Cdd:cd00029      1 HRFVPTTFSS-PTFCDVCGKLIWGLF---KQGLKCSDCGLVCHKKCLDKAPS-PC 50
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 810-1112 1.27e-05

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 49.08  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  810 LLVFVNVKSGGQTGKAIYKDLVAILNPLQV-IDIQAEGGPSRALSFFRPLAMTKRLRVLVCGGDGTVgwiidsihkvygA 888
Cdd:COG1597      5 ALLIVNPASGRGRAARLLERLVAALRAAGLeVEVLETESPGDATELAREAAAEGADLVVAAGGDGTV------------N 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  889 EAAEeergseaqtgdevdsgeaagkvgvesegrrgrresegVAWGSRdracdlrslVPVGICPLGTGNDLSNVLGwgfsF 968
Cdd:COG1597     73 EVAN-------------------------------------GLAGTG---------PPLGILPLGTGNDFARALG----I 102

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  969 DGDIMKHLLKIQSAVSSTLDLWKVkvisdktNATLvettFSNYLDVGVAARIVLKFHKLReenpelfQSRLGnKFLYGEV 1048
Cdd:COG1597    103 PLDPEAALEALLTGRTRRIDLGRV-------NGRY----FLNVAGIGFDAEVVERANRAL-------KRRLG-KLAYVLA 163

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379059808 1049 GFRDFLVTPNIALRglkIFCDGQEIALPYLeGICVVNIPSFAGGVELwdtAPEswaASASPGGL 1112
Cdd:COG1597    164 ALRALLRYRPFRLR---IELDGEEIEGEAL-LVAVGNGPYYGGGLRL---APD---ASLDDGLL 217
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 356-485 1.32e-05

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 50.38  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  356 VQGERGKTRLEGAHEKQREgkGDAHQLASEVEENRSTEQASGEAECRGNSGGSREAESGEDPL--ANEATRESKSVENES 433
Cdd:TIGR00927  740 EVEDEGEGEAEGKHEVETE--GDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKveHEGETEAGEKDEHEG 817

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1379059808  434 VDKEKEKDAQKKPREETCELVGEEEQEDAtrgdgSDNPPVDPGGKKDGGRSE 485
Cdd:TIGR00927  818 QSETQADDTEVKDETGEQELNAENQGEAK-----QDEKGVDGGGGSDGGDSE 864
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 158-207 4.51e-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: 42.45  E-value: 4.51e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1379059808   158 HQWEpFSSSSSPRYCSVCRQLISGfliYRNTGWACTLCQRYAHTKCLRLA 207
Cdd:smart00109    1 HKHV-FRTFTKPTFCCVCRKSIWG---SFKQGLRCSECKVKCHKKCADKV 46
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 381-742 1.23e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 47.32  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  381 QLASEVEENRSTEQASGEAECRGNSGGSREAESGEDPLANEATREsksvENESVDKEKEKDAQKKPREETCELVGEEEQE 460
Cdd:COG5271    423 DASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEE----DTESAEEDADGDEATDEDDASDDGDEEEAEE 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  461 DATRGDGSDNPPV-----DPGGKKDgGRSEPPRILSRFSESKGQPKPTTTARDSSTDSAAPSLTAASSDTQRLPEAEQTQ 535
Cdd:COG5271    499 DAEAEADSDELTAeetsaDDGADTD-AAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETED 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  536 DARSQRTDaspwgenKSTGGGQAGEAVEQHGDSAAIERGTGDREAAETSQPhgwAPDSSGETlHTPARDDPPCPHNARRK 615
Cdd:COG5271    578 ATENADAD-------ETEESADESEEAEASEDEAAEEEEADDDEADADADG---AADEEETE-EEAAEDEAAEPETDASE 646

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  616 LASTQRDEKQREGTAcllASAASsfachgppEPLGSHRPTAGAATSEEGDE-SRCQKTESENDGLGSGDVVRVGGFTDFT 694
Cdd:COG5271    647 AADEDADAETEAEAS---ADESE--------EEAEDESETSSEDAEEDADAaAAEASDDEEETEEADEDAETASEEADAE 715

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1379059808  695 EERSEEDLRTPSLEK---GSEGQDARQTEPDGRQKSGAPSEEALEKEDASV 742
Cdd:COG5271    716 EADTEADGTAEEAEEaaeEAESADEEAASLPDEADAEEEAEEAEEAEEDDA 766
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 316-476 2.85e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 45.76  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  316 KEVVKEGLREVQEGVRKFNEAIVQPLKKSLKF-EQRHSEQVVQGERGKTRLEgAHEKQREGKGDAHQLAS-------EVE 387
Cdd:pfam05262  198 RDMTDLKERESQEDAKRAQQLKEELDKKQIDAdKAQQKADFAQDNADKQRDE-VRQKQQEAKNLPKPADTsspkedkQVA 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  388 ENRSTEQASGEAECRGNSggsREAESGEDPLANEATRESKSVENESVDKEKEKDAQKKPREETCELVGEEEQEDATRGDG 467
Cdd:pfam05262  277 ENQKREIEKAQIEIKKND---EEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNE 353


                   ....*....
gi 1379059808  468 SDNPPVDPG 476
Cdd:pfam05262  354 DAIDSSNPV 362
PTZ00121 PTZ00121
MAEBL; Provisional
 312-469 7.75e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  312 RVGVKEVVKEGLREVQ--EGVRKFNEAIV---QPLKKSLKFEQRHSEQVVQGERGKTRLEGAHEKQREGKGDAHQL-ASE 385
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKkaEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkKKE 1711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  386 VEENRSTEQASGEAECRGNSGGSREAESGEDPLANEATRESKSVENESVDKEKEKDAQKKPREETCELVGEEE--QEDAT 463
Cdd:PTZ00121  1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEldEEDEK 1791


                   ....*.
gi 1379059808  464 RGDGSD 469
Cdd:PTZ00121  1792 RRMEVD 1797
PHA03169 PHA03169
hypothetical protein; Provisional
 478-723 8.37e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  478 KKDGGRSEPPRILSRFSESKGQPKPtttarDSSTDSAaPSLTAASSDTQRLPEAEQTQDARSQRTDASPWGENKSTGGGQ 557
Cdd:PHA03169    24 KRHGGTREQAGRRRGTAARAAKPAP-----PAPTTSG-PQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  558 AGEAVEQHGDSAAIERGT--GDREAAETSQPHGWA---PDSSGETLHTPARDDPPCPHNARRKLASTQRDEKQREGTAcL 632
Cdd:PHA03169    98 ESVGSPTPSPSGSAEELAsgLSPENTSGSSPESPAshsPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSP-E 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  633 LASAASSFACHGPPEPLGSHRPTAGAATSEEGDESrCQKTESENDGLGSGDVVRVGGFTDFTEERSEED-----LRTPSL 707
Cdd:PHA03169   177 EPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-GEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGppfpgHRSHSY 255

                          250
                   ....*....|....*.
gi 1379059808  708 EKGSEGQdarQTEPDG 723
Cdd:PHA03169   256 TVVGWKP---STRPGG 268
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1365-1544 5.04e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.81  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1365 EPAVELRGASPTDAGSRRRCVSEESREKRRLERTPVPDAGDRHEGDRGNlPSGSKASRSTADPEIAPAVAPQELSPKDSD 1444
Cdd:PRK12678   104 AAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQP-ATEARADAAERTEEEERDERRRRGDREDRQ 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1445 -GCTRDRQKKSQSKAAEEDDDSVDRPFAGSSQRKSRVScstsplKNRKTKDSHNRKRSARGAGRGVWHTRGQSLEDVSVS 1523
Cdd:PRK12678   183 aEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR------RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256

                          170       180
                   ....*....|....*....|.
gi 1379059808 1524 ELSPRRARRGRNVEERLRKGR 1544
Cdd:PRK12678   257 GRGGRRGRRFRDRDRRGRRGG 277
 
Name Accession Description Interval E-value
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1007-1109 8.58e-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: 116.55  E-value: 8.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1007 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTPNIALRG-LKIFCDGQEIALPY-LEGICVV 1084
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEkVELEVDGKDLPLPKsLEGIVVL 80

                           90       100
                   ....*....|....*....|....*
gi 1379059808 1085 NIPSFAGGVELWDTAPESWAASASP 1109
Cdd:pfam00609   81 NIPSYAGGTDLWGNSKEDGLGFAPQ 105
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 1007-1102 4.42e-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: 106.27  E-value: 4.42e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  1007 TFSNYLDVGVAARIVLKFHKLREENPELFQSRLGNKFLYGEVGFRDFLVTP--NIALRgLKIFCDGQEIALPY-LEGICV 1083
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTckDLHER-IELECDGVDVDLPNsLEGIAV 79

                            90
                    ....*....|....*....
gi 1379059808  1084 VNIPSFAGGVELWDTAPES 1102
Cdd:smart00045   80 LNIPSYGGGTNLWGTTDKE 98
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 223-277 1.30e-22

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: 92.51  E-value: 1.30e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPLCDLG 277
Cdd:cd20805      1 HHWVEGNLPSGAKCSVCGKKCGSSFGLAGYRCSWCKRTVHSECIDKLGPEECDLG 55
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 811-983 2.61e-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: 93.90  E-value: 2.61e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808   811 LVFVNVKSGGQTGKAIYKDLVAILNPLQVIDIQaEGGPSRALSFFRPLAmtKRLRVLVCGGDGTVGWIIDSIhkvygaea 890
Cdd:smart00046    1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLT-KKGPAVALVIFRDVP--DFNRVLVCGGDGTVGWVLNAL-------- 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808   891 aeeergseAQTGDEVDSgeaagkvgvesegrrgrresegvawgsrdracdlrslVPVGICPLGTGNDLSNVLGWGFSFDG 970
Cdd:smart00046   70 --------DKRELPLPE-------------------------------------PPVAVLPLGTGNDLARSLGWGGGYDG 104

                           170
                    ....*....|....*..
gi 1379059808   971 D----IMKHLLKIQSAV 983
Cdd:smart00046  105 EkllkTLRDALESDTVK 121
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 809-992 6.77e-20

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: 87.26  E-value: 6.77e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  809 PLLVFVNVKSGGQTGKAIYKDLVAILNPLQV-IDIQAEGGPSRALSFFRPLAMTKRLRVLVCGGDGTVGWIIDsihkvyg 887
Cdd:pfam00781    1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLN------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  888 aeaaeeergseaqtgdevdsgeaagkvgvesegrrgrreseGVAWGSRDracdlrslVPVGICPLGTGNDLSNVLGWGfs 967
Cdd:pfam00781   74 -----------------------------------------GLAGLATR--------PPLGIIPLGTGNDFARALGIP-- 102

                          170       180
                   ....*....|....*....|....*
gi 1379059808  968 fdGDIMKHLLKIQSAVSSTLDLWKV 992
Cdd:pfam00781  103 --GDPEEALEAILKGQTRPVDVGKV 125
C1_DGKepsilon_typeIII_rpt2 cd20853
second protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 223-286 5.81e-18

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: 79.63  E-value: 5.81e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSpLCDLGPFRQLVLPP 286
Cdd:cd20853      1 HHWVRGNLPLCSVCCVCNEQCGNQPGLCDYRCCWCQRTVHDDCLAKLPK-ECDLGAFRNFIVPP 63
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 1703-1760 2.30e-17

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: 81.11  E-value: 2.30e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1379059808 1703 RWRQQIINDQLIEVVGFKSLFHLGQVQVGLAKPVRLCQGRDIQLVLPQEIPLQIDGEP 1760
Cdd:pfam00609  101 GFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
C1_DGKtheta_typeV_rpt3 cd20854
third protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 223-286 8.36e-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: 8.36e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPsPLCDLGPFRQLVLPP 286
Cdd:cd20854      1 HHWREGNLPSNSKCEVCKKSCGSSECLAGMRCEWCGITAHASCYKSLP-KECNFGRLRNIILPP 63
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 1707-1760 1.80e-09

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: 58.50  E-value: 1.80e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1379059808  1707 QIINDQLIEVVGFKSLFHLGQVQVGLAKPVRLCQGRDIQLVL--PQEIPLQIDGEP 1760
Cdd:smart00045  105 QSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIktSKTIPMQVDGEP 160
C1_DGKdelta_rpt2 cd20893
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
 222-277 3.97e-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: 54.30  E-value: 3.97e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1379059808  222 PHVFIQGNLSAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPlCDLG 277
Cdd:cd20893      5 PHQWLEGNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKELLLTK-CPLG 59
C1_DGK_typeII_rpt2 cd20852
second protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
 223-277 4.50e-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: 4.50e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPlCDLG 277
Cdd:cd20852      1 HQWLEGNLPVSSKCAVCDKTCGSVLRLQDWRCLWCGATVHTACKDSLPTK-CSLG 54
C1_DGKalpha_rpt2 cd20890
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase alpha ...
 223-286 9.21e-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: 53.31  E-value: 9.21e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379059808  223 HVFIQGNLSAeATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPSPlCDLGPFRQLVLPP 286
Cdd:cd20890      1 HVWVSGGCES-SKCDKCQKKIKSFQSLTGLHCVWCHLKRHDECLSSVPST-CDCGPLRDHILPP 62
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 223-277 1.93e-08

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


Pssm-ID: 395079  Cd Length: 53  Bit Score: 52.06  E-value: 1.93e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSnFGLDGLRCLWCNRTLHEECRHRLPsPLCDLG 277
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWG-LGKQGLKCSWCKLNVHKRCHEKVP-PECGCD 53
C1_DGKeta_rpt2 cd20894
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
 222-280 1.09e-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: 50.29  E-value: 1.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1379059808  222 PHVFIQGNLSAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECRHRLPsPLCDLGPFR 280
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; ...
 223-277 2.70e-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: 2.70e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  223 HVFIQGNlsAEATCCCCGLACSSNFGLDGLRCLWCNRTLHEECrHRLPSPLCDLG 277
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 ...
 223-280 5.87e-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: 48.06  E-value: 5.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSnfGLDGLRCLWCNRTLHEECRHRLpSPLCDLGPFR 280
Cdd:cd20891      3 HFWVEGNCPTKCDKCHKTIKCYQ--GLTGLHCVWCQITLHNKCASHV-KPECDCGPLK 57
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 158-207 5.91e-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: 47.82  E-value: 5.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1379059808  158 HQWEPFSSSSsPRYCSVCRQLISGFliyRNTGWACTLCQRYAHTKCLRLA 207
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 ...
 158-212 6.21e-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: 6.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  158 HQWEPFSSSSsPRYCSVCRQLISGFLiyrNTGWACTLCQRYAHTKCLRLAERlDC 212
Cdd:cd00029      1 HRFVPTTFSS-PTFCDVCGKLIWGLF---KQGLKCSDCGLVCHKKCLDKAPS-PC 50
C1_DGKgamma_rpt2 cd20892
second protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
 223-286 7.08e-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: 45.19  E-value: 7.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSnfGLDGLRCLWCNRTLHEECrHRLPSPLCDLGPFRQLVLPP 286
Cdd:cd20892      1 HVWVEGNSPVKCDRCHKSIKCYQ--GLTGLHCVWCQITLHNKC-ASHVSPECDGGQLKDHILLP 61
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 810-1112 1.27e-05

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 49.08  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  810 LLVFVNVKSGGQTGKAIYKDLVAILNPLQV-IDIQAEGGPSRALSFFRPLAMTKRLRVLVCGGDGTVgwiidsihkvygA 888
Cdd:COG1597      5 ALLIVNPASGRGRAARLLERLVAALRAAGLeVEVLETESPGDATELAREAAAEGADLVVAAGGDGTV------------N 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  889 EAAEeergseaqtgdevdsgeaagkvgvesegrrgrresegVAWGSRdracdlrslVPVGICPLGTGNDLSNVLGwgfsF 968
Cdd:COG1597     73 EVAN-------------------------------------GLAGTG---------PPLGILPLGTGNDFARALG----I 102

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  969 DGDIMKHLLKIQSAVSSTLDLWKVkvisdktNATLvettFSNYLDVGVAARIVLKFHKLReenpelfQSRLGnKFLYGEV 1048
Cdd:COG1597    103 PLDPEAALEALLTGRTRRIDLGRV-------NGRY----FLNVAGIGFDAEVVERANRAL-------KRRLG-KLAYVLA 163

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379059808 1049 GFRDFLVTPNIALRglkIFCDGQEIALPYLeGICVVNIPSFAGGVELwdtAPEswaASASPGGL 1112
Cdd:COG1597    164 ALRALLRYRPFRLR---IELDGEEIEGEAL-LVAVGNGPYYGGGLRL---APD---ASLDDGLL 217
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 356-485 1.32e-05

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 50.38  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  356 VQGERGKTRLEGAHEKQREgkGDAHQLASEVEENRSTEQASGEAECRGNSGGSREAESGEDPL--ANEATRESKSVENES 433
Cdd:TIGR00927  740 EVEDEGEGEAEGKHEVETE--GDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKveHEGETEAGEKDEHEG 817

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1379059808  434 VDKEKEKDAQKKPREETCELVGEEEQEDAtrgdgSDNPPVDPGGKKDGGRSE 485
Cdd:TIGR00927  818 QSETQADDTEVKDETGEQELNAENQGEAK-----QDEKGVDGGGGSDGGDSE 864
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 158-207 4.51e-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: 42.45  E-value: 4.51e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1379059808   158 HQWEpFSSSSSPRYCSVCRQLISGfliYRNTGWACTLCQRYAHTKCLRLA 207
Cdd:smart00109    1 HKHV-FRTFTKPTFCCVCRKSIWG---SFKQGLRCSECKVKCHKKCADKV 46
C1_DGK_rpt2 cd20805
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ...
 171-212 6.08e-05

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


Pssm-ID: 410355  Cd Length: 55  Bit Score: 42.43  E-value: 6.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1379059808  171 YCSVCRQLISGflIYRNTGWACTLCQRYAHTKCLRLAERLDC 212
Cdd:cd20805     13 KCSVCGKKCGS--SFGLAGYRCSWCKRTVHSECIDKLGPEEC 52
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 381-742 1.23e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 47.32  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  381 QLASEVEENRSTEQASGEAECRGNSGGSREAESGEDPLANEATREsksvENESVDKEKEKDAQKKPREETCELVGEEEQE 460
Cdd:COG5271    423 DASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEE----DTESAEEDADGDEATDEDDASDDGDEEEAEE 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  461 DATRGDGSDNPPV-----DPGGKKDgGRSEPPRILSRFSESKGQPKPTTTARDSSTDSAAPSLTAASSDTQRLPEAEQTQ 535
Cdd:COG5271    499 DAEAEADSDELTAeetsaDDGADTD-AAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETED 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  536 DARSQRTDaspwgenKSTGGGQAGEAVEQHGDSAAIERGTGDREAAETSQPhgwAPDSSGETlHTPARDDPPCPHNARRK 615
Cdd:COG5271    578 ATENADAD-------ETEESADESEEAEASEDEAAEEEEADDDEADADADG---AADEEETE-EEAAEDEAAEPETDASE 646

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  616 LASTQRDEKQREGTAcllASAASsfachgppEPLGSHRPTAGAATSEEGDE-SRCQKTESENDGLGSGDVVRVGGFTDFT 694
Cdd:COG5271    647 AADEDADAETEAEAS---ADESE--------EEAEDESETSSEDAEEDADAaAAEASDDEEETEEADEDAETASEEADAE 715

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1379059808  695 EERSEEDLRTPSLEK---GSEGQDARQTEPDGRQKSGAPSEEALEKEDASV 742
Cdd:COG5271    716 EADTEADGTAEEAEEaaeEAESADEEAASLPDEADAEEEAEEAEEAEEDDA 766
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 223-272 1.39e-04

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: 40.96  E-value: 1.39e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1379059808  223 HVFIQGNLSAEATCCCCGLACSSnFGLDGLRCLWCNRTLHEECRHRLPSP 272
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWG-LFKQGLKCSDCGLVCHKKCLDKAPSP 49
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
 155-213 2.05e-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: 40.76  E-value: 2.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1379059808  155 KSLHQWEPFSSSSSPRYCSVCRQLI-SGFLiyrntgwaCTLCQRYAHTKCLRLAER-LDCK 213
Cdd:cd20801      1 SKGHHWVSTDLFSKPTYCSVCETLIlSGAF--------CDCCGLCVDEGCLRKADKrFPCK 53
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 316-476 2.85e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 45.76  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  316 KEVVKEGLREVQEGVRKFNEAIVQPLKKSLKF-EQRHSEQVVQGERGKTRLEgAHEKQREGKGDAHQLAS-------EVE 387
Cdd:pfam05262  198 RDMTDLKERESQEDAKRAQQLKEELDKKQIDAdKAQQKADFAQDNADKQRDE-VRQKQQEAKNLPKPADTsspkedkQVA 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  388 ENRSTEQASGEAECRGNSggsREAESGEDPLANEATRESKSVENESVDKEKEKDAQKKPREETCELVGEEEQEDATRGDG 467
Cdd:pfam05262  277 ENQKREIEKAQIEIKKND---EEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNE 353


                   ....*....
gi 1379059808  468 SDNPPVDPG 476
Cdd:pfam05262  354 DAIDSSNPV 362
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
 158-207 6.42e-04

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: 39.66  E-value: 6.42e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1379059808  158 HQWEPfSSSSSPRYCSVCRQLISGFliyRNTGWACTLCQRYAHTKCLRLA 207
Cdd:cd20799      6 HVWRL-KHFNKPAYCNVCENMLVGL---RKQGLCCTFCKYTVHERCVSRA 51
PTZ00121 PTZ00121
MAEBL; Provisional
 312-469 7.75e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  312 RVGVKEVVKEGLREVQ--EGVRKFNEAIV---QPLKKSLKFEQRHSEQVVQGERGKTRLEGAHEKQREGKGDAHQL-ASE 385
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKkaEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkKKE 1711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  386 VEENRSTEQASGEAECRGNSGGSREAESGEDPLANEATRESKSVENESVDKEKEKDAQKKPREETCELVGEEE--QEDAT 463
Cdd:PTZ00121  1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEldEEDEK 1791


                   ....*.
gi 1379059808  464 RGDGSD 469
Cdd:PTZ00121  1792 RRMEVD 1797
PHA03169 PHA03169
hypothetical protein; Provisional
 478-723 8.37e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  478 KKDGGRSEPPRILSRFSESKGQPKPtttarDSSTDSAaPSLTAASSDTQRLPEAEQTQDARSQRTDASPWGENKSTGGGQ 557
Cdd:PHA03169    24 KRHGGTREQAGRRRGTAARAAKPAP-----PAPTTSG-PQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  558 AGEAVEQHGDSAAIERGT--GDREAAETSQPHGWA---PDSSGETLHTPARDDPPCPHNARRKLASTQRDEKQREGTAcL 632
Cdd:PHA03169    98 ESVGSPTPSPSGSAEELAsgLSPENTSGSSPESPAshsPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSP-E 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  633 LASAASSFACHGPPEPLGSHRPTAGAATSEEGDESrCQKTESENDGLGSGDVVRVGGFTDFTEERSEED-----LRTPSL 707
Cdd:PHA03169   177 EPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-GEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGppfpgHRSHSY 255

                          250
                   ....*....|....*.
gi 1379059808  708 EKGSEGQdarQTEPDG 723
Cdd:PHA03169   256 TVVGWKP---STRPGG 268
PHA03169 PHA03169
hypothetical protein; Provisional
 357-593 2.25e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  357 QGERGKTRLEGAHEKQREGKGdahqlaSEVEENRSTEQASGEAecrGNSGGSREAESGEDPlaneATRESKSVENESVDK 436
Cdd:PHA03169    54 SGPQVRAVAEQGHRQTESDTE------TAEESRHGEKEERGQG---GPSGSGSESVGSPTP----SPSGSAEELASGLSP 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  437 EKEKDAQKKPREETcelvGEEEQEDATRGDGSDNPPVDPGGkkdggrsepprilsrfsesKGQPKPTTTARDSSTDSAAP 516
Cdd:PHA03169   121 ENTSGSSPESPASH----SPPPSPPSHPGPHEPAPPESHNP-------------------SPNQQPSSFLQPSHEDSPEE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  517 SLTAASSDTQRLPEAEQTQDARSQRTDASPW---GENKSTGGGQAGEAVEQHGDSAAIERGTGDREAAETSQPH------ 587
Cdd:PHA03169   178 PEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdepGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRshsytv 257


                   ....*..
gi 1379059808  588 -GWAPDS 593
Cdd:PHA03169   258 vGWKPST 264
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
 169-213 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 1379059808  169 PRYCSVCRQLISGfLIYRntGWACTLCQRYAHTKCLRLAERldCK 213
Cdd:cd20810     13 PTTCSVCKKLLKG-LFFQ--GYKCSVCGAAVHKECIAKVKR--CG 52
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 169-203 3.09e-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: 37.69  E-value: 3.09e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1379059808  169 PRYCSVCRQLISGFliyRNTGWACTLCQRYAHTKC 203
Cdd:cd20834     18 PTFCSVCKEFLWGF---NKQGYQCRQCNAAVHKKC 49
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 358-582 4.64e-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: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  358 GERGKTRLEGAHEKQREGKGDAHQlaSEVEENRSTEQASGE--AECRGNSGGSREAESGEDPLANEATRES----KSVEN 431
Cdd:TIGR00927  646 GEEGERPTEAEGENGEESGGEAEQ--EGETETKGENESEGEipAERKGEQEGEGEIEAKEADHKGETEAEEveheGETEA 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  432 ESVDKEKEKDAQKKPREETCELVGEEE--QEDATRGDGSD-NPPVDPGGKKDGGRSEPPRILSRFSESKGQPKPTTTARD 508
Cdd:TIGR00927  724 EGTEDEGEIETGEEGEEVEDEGEGEAEgkHEVETEGDRKEtEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEH 803

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1379059808  509 SSTDSAAPSLTAASSDTQRLPEAEQTQDARSQRTDASPWGENKSTGGGQAGEAVEQHGDSAAIERGTGDREAAE 582
Cdd:TIGR00927  804 EGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEE 877
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1365-1544 5.04e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.81  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1365 EPAVELRGASPTDAGSRRRCVSEESREKRRLERTPVPDAGDRHEGDRGNlPSGSKASRSTADPEIAPAVAPQELSPKDSD 1444
Cdd:PRK12678   104 AAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQP-ATEARADAAERTEEEERDERRRRGDREDRQ 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808 1445 -GCTRDRQKKSQSKAAEEDDDSVDRPFAGSSQRKSRVScstsplKNRKTKDSHNRKRSARGAGRGVWHTRGQSLEDVSVS 1523
Cdd:PRK12678   183 aEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR------RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256

                          170       180
                   ....*....|....*....|.
gi 1379059808 1524 ELSPRRARRGRNVEERLRKGR 1544
Cdd:PRK12678   257 GRGGRRGRRFRDRDRRGRRGG 277
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
 171-204 5.36e-03

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: 36.50  E-value: 5.36e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1379059808  171 YCSVCRQLIsgFliyrnTGWACTLCQRYAHTKCL 204
Cdd:cd20811     15 FCDVCRKLL--F-----QGFRCQTCGFKFHQRCS 41
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 415-622 7.09e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.12  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  415 EDPlanEATRESKSVENESVDKEkekdaqkkPREETCElvgeeeqedATRGDGSDNPPVDPGGKKDGGRSepprilsrfs 494
Cdd:PRK13108   280 EAP---GALRGSEYVVDEALERE--------PAELAAA---------AVASAASAVGPVGPGEPNQPDDV---------- 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379059808  495 eskGQPKPTTTARDSSTDSAAPSLTAASSDTQRLPEAEQTQDARSQR-----TDASPWGENKSTGGGQAgEAVEQHGDSA 569
Cdd:PRK13108   330 ---AEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEReqpgdLAGQAPAAHQVDAEAAS-AAPEEPAALA 405

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1379059808  570 AIERGTGDREAAETSQPHGwAPDSSGETLHTPARDDPPCPHNARR--KLASTQRD 622
Cdd:PRK13108   406 SEAHDETEPEVPEKAAPIP-DPAKPDELAVAGPGDDPAEPDGIRRqdDFSSRRRR 459
 
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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