PEBP (phosphatidylethanolamine-binding protein) family protein [Arabidopsis thaliana]
YbhB/YbcL family Raf kinase inhibitor-like protein( domain architecture ID 10791264)
YbhB/YbcL family Raf kinase inhibitor-like protein similar to Arabidopsis thaliana protein FLOWERING LOCUS T and protein TWIN SISTER of FT
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
PLN00169 | PLN00169 | CETS family protein; Provisional |
1-175 | 3.91e-129 | ||||
CETS family protein; Provisional : Pssm-ID: 177765 Cd Length: 175 Bit Score: 359.12 E-value: 3.91e-129
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
PLN00169 | PLN00169 | CETS family protein; Provisional |
1-175 | 3.91e-129 | ||||
CETS family protein; Provisional Pssm-ID: 177765 Cd Length: 175 Bit Score: 359.12 E-value: 3.91e-129
|
||||||||
PEBP_euk | cd00866 | PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ... |
26-164 | 1.07e-46 | ||||
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). The members in this subgroup are present in eukaryotes. Members here include those in plants such as Arabidopsis thaliana FLOWERING LOCUS (FT) and TERMINAL FLOWER1 (FT1) which function as a promoter and a repressor of the floral transitions, respectively as well as the mammalian Raf kinase inhibitory protein (RKIP) which inhibits MAP kinase (Raf-MEK-ERK), G protein-coupled receptor (GPCR) kinase and NFkappaB signaling cascades. Although their overall structures are similar, the members of the PEBP family have very different substrates and oligomerization states (monomer/dimer/tetramer). Pssm-ID: 176644 [Multi-domain] Cd Length: 154 Bit Score: 149.83 E-value: 1.07e-46
|
||||||||
PBP | pfam01161 | Phosphatidylethanolamine-binding protein; |
65-127 | 9.90e-12 | ||||
Phosphatidylethanolamine-binding protein; Pssm-ID: 460090 Cd Length: 136 Bit Score: 59.28 E-value: 9.90e-12
|
||||||||
PEBP | COG1881 | Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ... |
65-125 | 2.02e-07 | ||||
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family [General function prediction only]; Pssm-ID: 441485 Cd Length: 151 Bit Score: 47.84 E-value: 2.02e-07
|
||||||||
TIGR00481 | TIGR00481 | Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General] |
65-135 | 9.20e-04 | ||||
Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General] Pssm-ID: 129572 Cd Length: 141 Bit Score: 37.85 E-value: 9.20e-04
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
PLN00169 | PLN00169 | CETS family protein; Provisional |
1-175 | 3.91e-129 | ||||
CETS family protein; Provisional Pssm-ID: 177765 Cd Length: 175 Bit Score: 359.12 E-value: 3.91e-129
|
||||||||
PEBP_euk | cd00866 | PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ... |
26-164 | 1.07e-46 | ||||
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). The members in this subgroup are present in eukaryotes. Members here include those in plants such as Arabidopsis thaliana FLOWERING LOCUS (FT) and TERMINAL FLOWER1 (FT1) which function as a promoter and a repressor of the floral transitions, respectively as well as the mammalian Raf kinase inhibitory protein (RKIP) which inhibits MAP kinase (Raf-MEK-ERK), G protein-coupled receptor (GPCR) kinase and NFkappaB signaling cascades. Although their overall structures are similar, the members of the PEBP family have very different substrates and oligomerization states (monomer/dimer/tetramer). Pssm-ID: 176644 [Multi-domain] Cd Length: 154 Bit Score: 149.83 E-value: 1.07e-46
|
||||||||
PEBP | cd00457 | PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ... |
57-164 | 6.17e-17 | ||||
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). A number of biological roles for members of the PEBP family include serine protease inhibition, membrane biogenesis, regulation of flowering plant stem architecture, and Raf-1 kinase inhibition. Although their overall structures are similar, the members of the PEBP family bind very different substrates including phospholipids, opioids, and hydrophobic odorant molecules as well as having different oligomerization states (monomer/dimer/tetramer). Pssm-ID: 176642 Cd Length: 159 Bit Score: 73.58 E-value: 6.17e-17
|
||||||||
PBP | pfam01161 | Phosphatidylethanolamine-binding protein; |
65-127 | 9.90e-12 | ||||
Phosphatidylethanolamine-binding protein; Pssm-ID: 460090 Cd Length: 136 Bit Score: 59.28 E-value: 9.90e-12
|
||||||||
PEBP | COG1881 | Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ... |
65-125 | 2.02e-07 | ||||
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family [General function prediction only]; Pssm-ID: 441485 Cd Length: 151 Bit Score: 47.84 E-value: 2.02e-07
|
||||||||
PEBP_bact_arch | cd00865 | PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea; ... |
65-135 | 9.56e-06 | ||||
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea; PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). The members in this subgroup are present in bacterial and archaea. Members here include Escherichia coli YBHB and YBCL which are thought to regulate protein phosphorylation as well as Sulfolobus solfataricus SsCEI which inhibits serine proteases alpha-chymotrypsin and elastase. Although their overall structures are similar, the members of the PEBP family have very different substrates and oligomerization states (monomer/dimer/tetramer). In a few of the bacterial members present here the dimerization interface is proposed to form the ligand binding site, unlike in other PEBP members. Pssm-ID: 176643 Cd Length: 150 Bit Score: 43.36 E-value: 9.56e-06
|
||||||||
TIGR00481 | TIGR00481 | Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General] |
65-135 | 9.20e-04 | ||||
Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General] Pssm-ID: 129572 Cd Length: 141 Bit Score: 37.85 E-value: 9.20e-04
|
||||||||
Blast search parameters | ||||
|