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Conserved domains on  [gi|15237061|ref|NP_193770|]
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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 10791264)

YbhB/YbcL family Raf kinase inhibitor-like protein similar to Arabidopsis thaliana protein FLOWERING LOCUS T and protein TWIN SISTER of FT

CATH:  3.90.280.10
SCOP:  4002457

Graphical summary

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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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061    1 MSLSRRDPLVVGSVVGDVLDPFTRLVSLKVTYGHREVTNGLDLRPSQVLNKPIVEIGGDDFRNFYTLVMVDPDVPSPSNP 80
Cdd:PLN00169   1 MSPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061   81 HQREYLHWLVTDIPATTGNAFGNEVVCYESPRPPSGIHRIVLVLFRQLGRQTVYAPGWRQQFNTREFAEIYNLGLPVAAS 160
Cdd:PLN00169  81 NLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDFAELYNLGSPVAAV 160
                        170
                 ....*....|....*
gi 15237061  161 YFNCQRENGCGGRRT 175
Cdd:PLN00169 161 YFNCQRESGSGGRRP 175
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061    1 MSLSRRDPLVVGSVVGDVLDPFTRLVSLKVTYGHREVTNGLDLRPSQVLNKPIVEIGGDDFRNFYTLVMVDPDVPSPSNP 80
Cdd:PLN00169   1 MSPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061   81 HQREYLHWLVTDIPATTGNAFGNEVVCYESPRPPSGIHRIVLVLFRQLGRQTVYAPGWRQQFNTREFAEIYNLGLPVAAS 160
Cdd:PLN00169  81 NLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDFAELYNLGSPVAAV 160
                        170
                 ....*....|....*
gi 15237061  161 YFNCQRENGCGGRRT 175
Cdd:PLN00169 161 YFNCQRESGSGGRRP 175
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061  26 VSLKVTYG-HREVTNGLDLRPSQVLNKPIVEIGGDDFRN-FYTLVMVDPDVPSPSNPHQREYLHWLVTDIPATTGN---- 99
Cdd:cd00866   1 VDLTVSYGsSGVVTPGNLLTPSETQKAPTVSFSSEDPPDkLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTTtglv 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237061 100 AFGNEVVCYESPRPP--SGIHRIVLVLFRQLGRQTVYAPG-------WRQQFNTREFAEIYNLGLPVAASYFNC 164
Cdd:cd00866  81 SKGEVLVPYLGPGPPkgTGPHRYVFLLFKQPGGLDFPESKlpptsglGRRGFDVREFAKKNGLGLPVAANFFQV 154
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
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15237061    65 YTLVMVDPDVPSPSnphQREYLHWLVTDIPATTG--------------NAFGNEVvcYESPRPP--SGIHRIVLVLFRQ 127
Cdd:pfam01161  29 FALVMIDPDAPKVG---GSGWLHWVVTNIPATVTelpegapagavqglNDFGGAG--YGGPCPPagDGPHRYVFTLYAL 102
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061  65 YTLVMVDPDVPSPSNphqreYLHWLVTDIPATTG-------------------NAFGNevVCYESPRPPSG--IHRIVLV 123
Cdd:COG1881  41 FALIVEDPDAPTGGG-----FWHWVVYNIPADVTelpegagsadlpagavqgrNDFGE--AGYGGPCPPPGdgPHRYVFT 113

                ..
gi 15237061 124 LF 125
Cdd:COG1881 114 VY 115
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061    65 YTLVMVDPDVPSPSNphqreYLHWLVTDIPATTG----------------------NAFGNEVvcYESPRPPSGIHRIVL 122
Cdd:TIGR00481  30 LALTCIDPDAPTGCG-----WWHWVVVNIPADTTvlpenassddkrlpqgvplqgrNDFGKSG--YIGPCPPKGDHRYLF 102
                          90
                  ....*....|...
gi 15237061   123 vlfrqlgrqTVYA 135
Cdd:TIGR00481 103 ---------TVYA 106
 
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061    1 MSLSRRDPLVVGSVVGDVLDPFTRLVSLKVTYGHREVTNGLDLRPSQVLNKPIVEIGGDDFRNFYTLVMVDPDVPSPSNP 80
Cdd:PLN00169   1 MSPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061   81 HQREYLHWLVTDIPATTGNAFGNEVVCYESPRPPSGIHRIVLVLFRQLGRQTVYAPGWRQQFNTREFAEIYNLGLPVAAS 160
Cdd:PLN00169  81 NLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDFAELYNLGSPVAAV 160
                        170
                 ....*....|....*
gi 15237061  161 YFNCQRENGCGGRRT 175
Cdd:PLN00169 161 YFNCQRESGSGGRRP 175
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061  26 VSLKVTYG-HREVTNGLDLRPSQVLNKPIVEIGGDDFRN-FYTLVMVDPDVPSPSNPHQREYLHWLVTDIPATTGN---- 99
Cdd:cd00866   1 VDLTVSYGsSGVVTPGNLLTPSETQKAPTVSFSSEDPPDkLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTTtglv 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237061 100 AFGNEVVCYESPRPP--SGIHRIVLVLFRQLGRQTVYAPG-------WRQQFNTREFAEIYNLGLPVAASYFNC 164
Cdd:cd00866  81 SKGEVLVPYLGPGPPkgTGPHRYVFLLFKQPGGLDFPESKlpptsglGRRGFDVREFAKKNGLGLPVAANFFQV 154
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061  57 GGDDFRNFYTLVMVDPDVPSPsnphqREYLHWLVTDIPATT------------GNAFGNEVVC----------YESPRPP 114
Cdd:cd00457  33 GPPPDVKEYVLVMEDPDAPLG-----RPIVHGLVYGIPANKtslsnddfvvtdNGKGGLQGGFkygknrggtvYIGPRPP 107
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15237061 115 --SGIHRIVLVLFRQLGRQTVYAPGW-RQQFNTREFAEIYNLGlPVAASYFNC 164
Cdd:cd00457 108 lgHGPHRYFFQVYALDEPLDRSKLGDgRTKFEVARFAEGNVLG-AVGEWVGQF 159
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
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15237061    65 YTLVMVDPDVPSPSnphQREYLHWLVTDIPATTG--------------NAFGNEVvcYESPRPP--SGIHRIVLVLFRQ 127
Cdd:pfam01161  29 FALVMIDPDAPKVG---GSGWLHWVVTNIPATVTelpegapagavqglNDFGGAG--YGGPCPPagDGPHRYVFTLYAL 102
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061  65 YTLVMVDPDVPSPSNphqreYLHWLVTDIPATTG-------------------NAFGNevVCYESPRPPSG--IHRIVLV 123
Cdd:COG1881  41 FALIVEDPDAPTGGG-----FWHWVVYNIPADVTelpegagsadlpagavqgrNDFGE--AGYGGPCPPPGdgPHRYVFT 113

                ..
gi 15237061 124 LF 125
Cdd:COG1881 114 VY 115
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
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061  65 YTLVMVDPDVPSPSnphqrEYLHWLVTDIPATTG-------------------NAFGNevVCYESPRPPS-GIHRIVLvl 124
Cdd:cd00865  42 LALIVEDPDAPTGG-----GFVHWVVWNIPADTTelpegasrgalpagavqgrNDFGE--AGYGGPCPPDgGPHRYVF-- 112
                        90
                ....*....|.
gi 15237061 125 frqlgrqTVYA 135
Cdd:cd00865 113 -------TVYA 116
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237061    65 YTLVMVDPDVPSPSNphqreYLHWLVTDIPATTG----------------------NAFGNEVvcYESPRPPSGIHRIVL 122
Cdd:TIGR00481  30 LALTCIDPDAPTGCG-----WWHWVVVNIPADTTvlpenassddkrlpqgvplqgrNDFGKSG--YIGPCPPKGDHRYLF 102
                          90
                  ....*....|...
gi 15237061   123 vlfrqlgrqTVYA 135
Cdd:TIGR00481 103 ---------TVYA 106
 
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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