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Conserved domains on  [gi|223997526|ref|XP_002288436|]
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predicted protein [Thalassiosira pseudonana CCMP1335]

Protein Classification

PH domain-containing protein; protein kinase family protein( domain architecture ID 10643953)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner| fungal protein kinase family protein containing a variant of the protein kinase domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EDR2_C pfam07059
Protein ENHANCED DISEASE RESISTANCE 2, C-terminal; This family represents the C-terminus ...
 757-1018 1.67e-47

Protein ENHANCED DISEASE RESISTANCE 2, C-terminal; This family represents the C-terminus (approximately 250 residues) of protein ENHANCED DISEASE RESISTANCE 2 (EDR2) from plants. EDR2 is a negative regulator of the salicylic acid (SA)-mediated resistance to pathogens, including the biotrophic powdery mildew pathogens Golovinomyces cichoracearum and Blumeria graminis, and the downy mildew pathogen Hyaloperonospora parasitica, probably by limiting the initiation of cell death and the establishment of the hypersensitive response (HR).


:

Pssm-ID: 462076  Cd Length: 211  Bit Score: 168.55  E-value: 1.67e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   757 WVPMQSSGLEVRSHGYLASKTKISAPADLYECIGTDCFASNARIPDIAPRVVLPDvqFSDGDSPKTW-KSPDIMVISVSI 835
Cdd:pfam07059    1 WSEPDGSTFKVRGPNYLKDKKKVPAGPPLYELVGVDLFKSPKKIDHIASRPELPV--ALKPSEKGASgKVPFVFVVNLQV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   836 PteapsfgkstddGQGTTMVGYFkmkeetrAILRRITaadydastdtaDDELDVQKRITNGvrlweryckqapNDPEFQA 915
Cdd:pfam07059   79 P------------GPGYSLVLYF-------ATEEPLP-----------DDEGSLLDRFVDG------------DDAFRNE 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   916 RFKLVPH-ANLVELGCPAyiakYNGKPVLIKRNQVTGFftdYPALNAMEFDISLHPFPYlFKQATSYLKEnYFDKAVVTF 994
Cdd:pfam07059  117 RFKLIPRiVNGPWIVKQA----VGGKPVLIGKALTCKY---HRGHNYFEIDVDIHSSSY-ARKGLSLVLG-YLKSLVVDL 187

                          250       260
                   ....*....|....*....|....
gi 223997526   995 GFVVEGRCDDELPEVMIGAMRVCY 1018
Cdd:pfam07059  188 GFTIEGQTEEELPERLLGAVRLNK 211
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 508-575 2.18e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


:

Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 47.16  E-value: 2.18e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223997526    508 EKPPSADTPRGILDISKerATVAASLGHSGSPTPFCISIKTRGQTTYKFCFDNHSIMMEWLAALTDVV 575
Cdd:smart00233   36 KKDKKSYKPKGSIDLSG--CTVREAPDPDSSKKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRKAI 101
 
Name Accession Description Interval E-value
EDR2_C pfam07059
Protein ENHANCED DISEASE RESISTANCE 2, C-terminal; This family represents the C-terminus ...
 757-1018 1.67e-47

Protein ENHANCED DISEASE RESISTANCE 2, C-terminal; This family represents the C-terminus (approximately 250 residues) of protein ENHANCED DISEASE RESISTANCE 2 (EDR2) from plants. EDR2 is a negative regulator of the salicylic acid (SA)-mediated resistance to pathogens, including the biotrophic powdery mildew pathogens Golovinomyces cichoracearum and Blumeria graminis, and the downy mildew pathogen Hyaloperonospora parasitica, probably by limiting the initiation of cell death and the establishment of the hypersensitive response (HR).


Pssm-ID: 462076  Cd Length: 211  Bit Score: 168.55  E-value: 1.67e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   757 WVPMQSSGLEVRSHGYLASKTKISAPADLYECIGTDCFASNARIPDIAPRVVLPDvqFSDGDSPKTW-KSPDIMVISVSI 835
Cdd:pfam07059    1 WSEPDGSTFKVRGPNYLKDKKKVPAGPPLYELVGVDLFKSPKKIDHIASRPELPV--ALKPSEKGASgKVPFVFVVNLQV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   836 PteapsfgkstddGQGTTMVGYFkmkeetrAILRRITaadydastdtaDDELDVQKRITNGvrlweryckqapNDPEFQA 915
Cdd:pfam07059   79 P------------GPGYSLVLYF-------ATEEPLP-----------DDEGSLLDRFVDG------------DDAFRNE 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   916 RFKLVPH-ANLVELGCPAyiakYNGKPVLIKRNQVTGFftdYPALNAMEFDISLHPFPYlFKQATSYLKEnYFDKAVVTF 994
Cdd:pfam07059  117 RFKLIPRiVNGPWIVKQA----VGGKPVLIGKALTCKY---HRGHNYFEIDVDIHSSSY-ARKGLSLVLG-YLKSLVVDL 187

                          250       260
                   ....*....|....*....|....
gi 223997526   995 GFVVEGRCDDELPEVMIGAMRVCY 1018
Cdd:pfam07059  188 GFTIEGQTEEELPERLLGAVRLNK 211
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 508-575 2.18e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 47.16  E-value: 2.18e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223997526    508 EKPPSADTPRGILDISKerATVAASLGHSGSPTPFCISIKTRGQTTYKFCFDNHSIMMEWLAALTDVV 575
Cdd:smart00233   36 KKDKKSYKPKGSIDLSG--CTVREAPDPDSSKKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 508-575 5.22e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 40.62  E-value: 5.22e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223997526   508 EKPPSADTPRGILDISKerATVAASLGHSGSPTPFCISIKT---RGQTTYKFCFDNHSIMMEWLAALTDVV 575
Cdd:pfam00169   36 DKSGKSKEPKGSISLSG--CEVVEVVASDSPKRKFCFELRTgerTGKRTYLLQAESEEERKDWIKAIQSAI 104
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 508-571 1.41e-03

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 39.06  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223997526  508 EKPPSADTPRGILDISKEratVAASLGHSGSPtPFCISIKTRGQTTYKFCFDNHSIMMEWLAAL 571
Cdd:cd00821    33 SKKDSSYKPKGSIPLSGI---LEVEEVSPKER-PHCFELVTPDGRTYYLQADSEEERQEWLKAL 92
 
Name Accession Description Interval E-value
EDR2_C pfam07059
Protein ENHANCED DISEASE RESISTANCE 2, C-terminal; This family represents the C-terminus ...
 757-1018 1.67e-47

Protein ENHANCED DISEASE RESISTANCE 2, C-terminal; This family represents the C-terminus (approximately 250 residues) of protein ENHANCED DISEASE RESISTANCE 2 (EDR2) from plants. EDR2 is a negative regulator of the salicylic acid (SA)-mediated resistance to pathogens, including the biotrophic powdery mildew pathogens Golovinomyces cichoracearum and Blumeria graminis, and the downy mildew pathogen Hyaloperonospora parasitica, probably by limiting the initiation of cell death and the establishment of the hypersensitive response (HR).


Pssm-ID: 462076  Cd Length: 211  Bit Score: 168.55  E-value: 1.67e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   757 WVPMQSSGLEVRSHGYLASKTKISAPADLYECIGTDCFASNARIPDIAPRVVLPDvqFSDGDSPKTW-KSPDIMVISVSI 835
Cdd:pfam07059    1 WSEPDGSTFKVRGPNYLKDKKKVPAGPPLYELVGVDLFKSPKKIDHIASRPELPV--ALKPSEKGASgKVPFVFVVNLQV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   836 PteapsfgkstddGQGTTMVGYFkmkeetrAILRRITaadydastdtaDDELDVQKRITNGvrlweryckqapNDPEFQA 915
Cdd:pfam07059   79 P------------GPGYSLVLYF-------ATEEPLP-----------DDEGSLLDRFVDG------------DDAFRNE 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223997526   916 RFKLVPH-ANLVELGCPAyiakYNGKPVLIKRNQVTGFftdYPALNAMEFDISLHPFPYlFKQATSYLKEnYFDKAVVTF 994
Cdd:pfam07059  117 RFKLIPRiVNGPWIVKQA----VGGKPVLIGKALTCKY---HRGHNYFEIDVDIHSSSY-ARKGLSLVLG-YLKSLVVDL 187

                          250       260
                   ....*....|....*....|....
gi 223997526   995 GFVVEGRCDDELPEVMIGAMRVCY 1018
Cdd:pfam07059  188 GFTIEGQTEEELPERLLGAVRLNK 211
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 508-575 2.18e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 47.16  E-value: 2.18e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223997526    508 EKPPSADTPRGILDISKerATVAASLGHSGSPTPFCISIKTRGQTTYKFCFDNHSIMMEWLAALTDVV 575
Cdd:smart00233   36 KKDKKSYKPKGSIDLSG--CTVREAPDPDSSKKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 508-575 5.22e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 40.62  E-value: 5.22e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223997526   508 EKPPSADTPRGILDISKerATVAASLGHSGSPTPFCISIKT---RGQTTYKFCFDNHSIMMEWLAALTDVV 575
Cdd:pfam00169   36 DKSGKSKEPKGSISLSG--CEVVEVVASDSPKRKFCFELRTgerTGKRTYLLQAESEEERKDWIKAIQSAI 104
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 508-571 1.41e-03

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 39.06  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223997526  508 EKPPSADTPRGILDISKEratVAASLGHSGSPtPFCISIKTRGQTTYKFCFDNHSIMMEWLAAL 571
Cdd:cd00821    33 SKKDSSYKPKGSIPLSGI---LEVEEVSPKER-PHCFELVTPDGRTYYLQADSEEERQEWLKAL 92
 
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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