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Conserved domains on  [gi|15237535|ref|NP_196004|]
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PEBP (phosphatidylethanolamine-binding protein) family protein [Arabidopsis thaliana]

Protein Classification

YbhB/YbcL family Raf kinase inhibitor-like protein( domain architecture ID 1002)

YbhB/YbcL family Raf kinase inhibitor-like protein similar to Arabidopsis thaliana protein BROTHER of FT and TFL 1 that may form complexes with phosphorylated ligands by interfering with kinases and their effectors

CATH:  3.90.280.10
SCOP:  4002457

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PEBP super family cl00227
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ...
 4-177 2.71e-83

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).


The actual alignment was detected with superfamily member PLN00169:

Pssm-ID: 469671  Cd Length: 175  Bit Score: 243.18  E-value: 2.71e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535    4 MGTRVIEPLIMGRVVGDVLDFFTPTTKMNVSYNKKQVSNGHELFPSSVSSKPRVEIHGGDLRSFFTLVMIDPDVPGPSDP 83
Cdd:PLN00169   1 MSPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535   84 FLKEHLHWIVTNIPGTTDATFGKEVVSYELPRPSIGIHRFVFVLFRQKQRRVIFPniPS-RDHFNTRKFAVEYDLGLPVA 162
Cdd:PLN00169  81 NLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYA--PGwRQNFNTRDFAELYNLGSPVA 158

                        170
                 ....*....|....*
gi 15237535  163 AVFFNAQRETAARKR 177
Cdd:PLN00169 159 AVYFNCQRESGSGGR 173
 
Name Accession Description Interval E-value
PLN00169 PLN00169
CETS family protein; Provisional
 4-177 2.71e-83

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 243.18  E-value: 2.71e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535    4 MGTRVIEPLIMGRVVGDVLDFFTPTTKMNVSYNKKQVSNGHELFPSSVSSKPRVEIHGGDLRSFFTLVMIDPDVPGPSDP 83
Cdd:PLN00169   1 MSPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535   84 FLKEHLHWIVTNIPGTTDATFGKEVVSYELPRPSIGIHRFVFVLFRQKQRRVIFPniPS-RDHFNTRKFAVEYDLGLPVA 162
Cdd:PLN00169  81 NLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYA--PGwRQNFNTRDFAELYNLGSPVA 158

                        170
                 ....*....|....*
gi 15237535  163 AVFFNAQRETAARKR 177
Cdd:PLN00169 159 AVYFNCQRESGSGGR 173
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 29-168 5.41e-42

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: 137.89  E-value: 5.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535  29 TKMNVSY-NKKQVSNGHELFPSSVSSKPRVEIHGGDLRS-FFTLVMIDPDVPGPSDPFLKEHLHWIVTNIPGTTDATF-- 104
Cdd:cd00866   1 VDLTVSYgSSGVVTPGNLLTPSETQKAPTVSFSSEDPPDkLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTTTGlv 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237535 105 --GKEVVSYELPRPSI--GIHRFVFVLFRQKQRRVIFPNIP------SRDHFNTRKFAVEYDLGLPVAAVFFNA 168
Cdd:cd00866  81 skGEVLVPYLGPGPPKgtGPHRYVFLLFKQPGGLDFPESKLpptsglGRRGFDVREFAKKNGLGLPVAANFFQV 154
PBP pfam01161
Phosphatidylethanolamine-binding protein;
68-166 4.82e-10

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 54.65  E-value: 4.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535    68 FTLVMIDPDVP-GPSDPFlkehLHWIVTNIPGTTDA--------------TFGKevVSYE--LPRPSIGIHRFVFVLFRQ 130
Cdd:pfam01161  29 FALVMIDPDAPkVGGSGW----LHWVVTNIPATVTElpegapagavqglnDFGG--AGYGgpCPPAGDGPHRYVFTLYAL 102

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15237535   131 KQRRVIFPNIPSRDHFNtRKFAvEYDLGLPVAAVFF 166
Cdd:pfam01161 103 DVPLLDRNWGFTKAELG-VAFA-GHVLALAVLAGNY 136
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 68-128 4.00e-07

Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family [General function prediction only];


Pssm-ID: 441485  Cd Length: 151  Bit Score: 47.07  E-value: 4.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535  68 FTLVMIDPDVPGPSdPFLkehlHWIVTNIPGTT--------------DATFGK---EVVSYELPRPSIG--IHRFVFVLF 128
Cdd:COG1881  41 FALIVEDPDAPTGG-GFW----HWVVYNIPADVtelpegagsadlpaGAVQGRndfGEAGYGGPCPPPGdgPHRYVFTVY 115
 
Name Accession Description Interval E-value
PLN00169 PLN00169
CETS family protein; Provisional
 4-177 2.71e-83

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 243.18  E-value: 2.71e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535    4 MGTRVIEPLIMGRVVGDVLDFFTPTTKMNVSYNKKQVSNGHELFPSSVSSKPRVEIHGGDLRSFFTLVMIDPDVPGPSDP 83
Cdd:PLN00169   1 MSPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535   84 FLKEHLHWIVTNIPGTTDATFGKEVVSYELPRPSIGIHRFVFVLFRQKQRRVIFPniPS-RDHFNTRKFAVEYDLGLPVA 162
Cdd:PLN00169  81 NLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYA--PGwRQNFNTRDFAELYNLGSPVA 158

                        170
                 ....*....|....*
gi 15237535  163 AVFFNAQRETAARKR 177
Cdd:PLN00169 159 AVYFNCQRESGSGGR 173
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 29-168 5.41e-42

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: 137.89  E-value: 5.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535  29 TKMNVSY-NKKQVSNGHELFPSSVSSKPRVEIHGGDLRS-FFTLVMIDPDVPGPSDPFLKEHLHWIVTNIPGTTDATF-- 104
Cdd:cd00866   1 VDLTVSYgSSGVVTPGNLLTPSETQKAPTVSFSSEDPPDkLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTTTGlv 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237535 105 --GKEVVSYELPRPSI--GIHRFVFVLFRQKQRRVIFPNIP------SRDHFNTRKFAVEYDLGLPVAAVFFNA 168
Cdd:cd00866  81 skGEVLVPYLGPGPPKgtGPHRYVFLLFKQPGGLDFPESKLpptsglGRRGFDVREFAKKNGLGLPVAANFFQV 154
PEBP cd00457
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ...
 43-168 2.33e-18

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: 77.44  E-value: 2.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535  43 GHELFP----SSVSSKPRVEIHGGD-LRSFFTLVMIDPDVPGPSdpflkEHLHWIVTNIPGTT------------DATFG 105
Cdd:cd00457  11 GSVLPPeysfEGVGRFPSLSWDGPPpDVKEYVLVMEDPDAPLGR-----PIVHGLVYGIPANKtslsnddfvvtdNGKGG 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15237535 106 KEVV----------SYELPRPSI--GIHRFVFVLFRQKQRRVIFPNIPSRDHFNTRKFAVEYDLGlPVAAVFFNA 168
Cdd:cd00457  86 LQGGfkygknrggtVYIGPRPPLghGPHRYFFQVYALDEPLDRSKLGDGRTKFEVARFAEGNVLG-AVGEWVGQF 159
PBP pfam01161
Phosphatidylethanolamine-binding protein;
68-166 4.82e-10

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 54.65  E-value: 4.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535    68 FTLVMIDPDVP-GPSDPFlkehLHWIVTNIPGTTDA--------------TFGKevVSYE--LPRPSIGIHRFVFVLFRQ 130
Cdd:pfam01161  29 FALVMIDPDAPkVGGSGW----LHWVVTNIPATVTElpegapagavqglnDFGG--AGYGgpCPPAGDGPHRYVFTLYAL 102

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15237535   131 KQRRVIFPNIPSRDHFNtRKFAvEYDLGLPVAAVFF 166
Cdd:pfam01161 103 DVPLLDRNWGFTKAELG-VAFA-GHVLALAVLAGNY 136
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 68-128 4.00e-07

Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family [General function prediction only];


Pssm-ID: 441485  Cd Length: 151  Bit Score: 47.07  E-value: 4.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237535  68 FTLVMIDPDVPGPSdPFLkehlHWIVTNIPGTT--------------DATFGK---EVVSYELPRPSIG--IHRFVFVLF 128
Cdd:COG1881  41 FALIVEDPDAPTGG-GFW----HWVVYNIPADVtelpegagsadlpaGAVQGRndfGEAGYGGPCPPPGdgPHRYVFTVY 115
PEBP_bact_arch cd00865
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea; ...
 68-128 1.61e-05

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: 42.59  E-value: 1.61e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15237535  68 FTLVMIDPDVPGPSdPFLkehlHWIVTNIPGTT--------------DATFGK---EVVSYELPRP-SIGIHRFVFVLF 128
Cdd:cd00865  42 LALIVEDPDAPTGG-GFV----HWVVWNIPADTtelpegasrgalpaGAVQGRndfGEAGYGGPCPpDGGPHRYVFTVY 115
 
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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