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Conserved domains on  [gi|1388875960|ref|NP_001350162|]
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phosphatidylethanolamine-binding protein 4 precursor [Homo sapiens]

Protein Classification

YbhB/YbcL family Raf kinase inhibitor-like protein( domain architecture ID 10096268)

YbhB/YbcL family Raf kinase inhibitor-like protein similar to mammalian phosphatidylethanolamine-binding protein 1/2 and Schizosaccharomyces pombe mitochondrial 54S ribosomal protein L35

CATH:  3.90.280.10
SCOP:  4002457

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 46-197 7.83e-40

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: 134.04  E-value: 7.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  46 LEVFYPelgniGCKVVPDCNNYRQKITsWMEPIVKFPGA-VDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKGADLK 124
Cdd:cd00866     3 LTVSYG-----SSGVVTPGNLLTPSET-QKAPTVSFSSEdPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388875960 125 KGKI-QGQELSAYQAPSPPAHSGFHRYQFFVYLQEGKVIS----LLPKENKTRGSWKMDRFLNRFHLGEPEASTQFMT 197
Cdd:cd00866    77 TGLVsKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFpeskLPPTSGLGRRGFDVREFAKKNGLGLPVAANFFQV 154
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 46-197 7.83e-40

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: 134.04  E-value: 7.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  46 LEVFYPelgniGCKVVPDCNNYRQKITsWMEPIVKFPGA-VDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKGADLK 124
Cdd:cd00866     3 LTVSYG-----SSGVVTPGNLLTPSET-QKAPTVSFSSEdPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388875960 125 KGKI-QGQELSAYQAPSPPAHSGFHRYQFFVYLQEGKVIS----LLPKENKTRGSWKMDRFLNRFHLGEPEASTQFMT 197
Cdd:cd00866    77 TGLVsKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFpeskLPPTSGLGRRGFDVREFAKKNGLGLPVAANFFQV 154
PLN00169 PLN00169
CETS family protein; Provisional
 76-198 4.08e-19

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 81.01  E-value: 4.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  76 EPIVKFPGAVDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKGAdlkKGKIQGQELSAYQAPSPPAhsGFHRYQFFVY 155
Cdd:PLN00169   51 QPRVDIGGEDLRTFYTLVMVDPDAPSPSNPNLREYLHWLVTDIPAT---TGATFGQEVVCYESPRPTA--GIHRFVFVLF 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1388875960 156 LQEGKVISLLPkenKTRGSWKMDRFLNRFHLGEPEASTQFMTQ 198
Cdd:PLN00169  126 RQLGRQTVYAP---GWRQNFNTRDFAELYNLGSPVAAVYFNCQ 165
PBP pfam01161
Phosphatidylethanolamine-binding protein;
77-155 5.45e-18

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 77.00  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  77 PIVKFPGAVDGA-TYILVMVDPDAPSRAEPRqrfWRHWLVTDIKG------ADLKKGKIQGQE---LSAYQAPSPPAHSG 146
Cdd:pfam01161  15 PPLAWSGAPAGTkSFALVMIDPDAPKVGGSG---WLHWVVTNIPAtvtelpEGAPAGAVQGLNdfgGAGYGGPCPPAGDG 91


                  ....*....
gi 1388875960 147 FHRYQFFVY 155
Cdd:pfam01161  92 PHRYVFTLY 100
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 83-155 3.74e-09

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


Pssm-ID: 441485  Cd Length: 151  Bit Score: 53.62  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  83 GAVDGA-TYILVMVDPDAPSRAEprqrfWRHWLVTDI--------KGA---DLKKGKIQGQ---ELSAYQAPSPPAHSGF 147
Cdd:COG1881    33 GAPEGTkSFALIVEDPDAPTGGG-----FWHWVVYNIpadvtelpEGAgsaDLPAGAVQGRndfGEAGYGGPCPPPGDGP 107


                  ....*...
gi 1388875960 148 HRYQFFVY 155
Cdd:COG1881   108 HRYVFTVY 115
TIGR00481 TIGR00481
Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General]
 77-155 5.93e-06

Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General]


Pssm-ID: 129572  Cd Length: 141  Bit Score: 44.40  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  77 PIVKFPGAVDGA-TYILVMVDPDAPSRAEprqrfWRHWLVTDI--------KGADLKKGKI-QGQEL--------SAYQA 138
Cdd:TIGR00481  16 PPLSWDGVPEGAkSLALTCIDPDAPTGCG-----WWHWVVVNIpadttvlpENASSDDKRLpQGVPLqgrndfgkSGYIG 90

                          90
                  ....*....|....*..
gi 1388875960 139 PSPPahSGFHRYQFFVY 155
Cdd:TIGR00481  91 PCPP--KGDHRYLFTVY 105
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 46-197 7.83e-40

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: 134.04  E-value: 7.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  46 LEVFYPelgniGCKVVPDCNNYRQKITsWMEPIVKFPGA-VDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKGADLK 124
Cdd:cd00866     3 LTVSYG-----SSGVVTPGNLLTPSET-QKAPTVSFSSEdPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388875960 125 KGKI-QGQELSAYQAPSPPAHSGFHRYQFFVYLQEGKVIS----LLPKENKTRGSWKMDRFLNRFHLGEPEASTQFMT 197
Cdd:cd00866    77 TGLVsKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFpeskLPPTSGLGRRGFDVREFAKKNGLGLPVAANFFQV 154
PLN00169 PLN00169
CETS family protein; Provisional
 76-198 4.08e-19

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 81.01  E-value: 4.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  76 EPIVKFPGAVDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKGAdlkKGKIQGQELSAYQAPSPPAhsGFHRYQFFVY 155
Cdd:PLN00169   51 QPRVDIGGEDLRTFYTLVMVDPDAPSPSNPNLREYLHWLVTDIPAT---TGATFGQEVVCYESPRPTA--GIHRFVFVLF 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1388875960 156 LQEGKVISLLPkenKTRGSWKMDRFLNRFHLGEPEASTQFMTQ 198
Cdd:PLN00169  126 RQLGRQTVYAP---GWRQNFNTRDFAELYNLGSPVAAVYFNCQ 165
PBP pfam01161
Phosphatidylethanolamine-binding protein;
77-155 5.45e-18

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 77.00  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  77 PIVKFPGAVDGA-TYILVMVDPDAPSRAEPRqrfWRHWLVTDIKG------ADLKKGKIQGQE---LSAYQAPSPPAHSG 146
Cdd:pfam01161  15 PPLAWSGAPAGTkSFALVMIDPDAPKVGGSG---WLHWVVTNIPAtvtelpEGAPAGAVQGLNdfgGAGYGGPCPPAGDG 91


                  ....*....
gi 1388875960 147 FHRYQFFVY 155
Cdd:pfam01161  92 PHRYVFTLY 100
PEBP cd00457
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ...
 77-171 5.96e-13

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: 64.34  E-value: 5.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  77 PIVKFPG-AVDGATYILVMVDPDAPSRAEprqrfWRHWLVTDIKG------------ADLKKGKIQG-------QELSAY 136
Cdd:cd00457    27 PSLSWDGpPPDVKEYVLVMEDPDAPLGRP-----IVHGLVYGIPAnktslsnddfvvTDNGKGGLQGgfkygknRGGTVY 101

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1388875960 137 QAPSPPAHSGFHRYQFFVYLQEGKVISLLPKENKT 171
Cdd:cd00457   102 IGPRPPLGHGPHRYFFQVYALDEPLDRSKLGDGRT 136
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 83-155 3.74e-09

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


Pssm-ID: 441485  Cd Length: 151  Bit Score: 53.62  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  83 GAVDGA-TYILVMVDPDAPSRAEprqrfWRHWLVTDI--------KGA---DLKKGKIQGQ---ELSAYQAPSPPAHSGF 147
Cdd:COG1881    33 GAPEGTkSFALIVEDPDAPTGGG-----FWHWVVYNIpadvtelpEGAgsaDLPAGAVQGRndfGEAGYGGPCPPPGDGP 107


                  ....*...
gi 1388875960 148 HRYQFFVY 155
Cdd:COG1881   108 HRYVFTVY 115
PEBP_bact_arch cd00865
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea; ...
 88-155 4.19e-08

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: 50.68  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  88 ATYILVMVDPDAPSRAEprqrfWRHWLVTDIKG-----------ADLKKGKIQGQ---ELSAYQAPSPPAHsGFHRYQFF 153
Cdd:cd00865    40 KSLALIVEDPDAPTGGG-----FVHWVVWNIPAdttelpegasrGALPAGAVQGRndfGEAGYGGPCPPDG-GPHRYVFT 113


                  ..
gi 1388875960 154 VY 155
Cdd:cd00865   114 VY 115
TIGR00481 TIGR00481
Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General]
 77-155 5.93e-06

Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General]


Pssm-ID: 129572  Cd Length: 141  Bit Score: 44.40  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  77 PIVKFPGAVDGA-TYILVMVDPDAPSRAEprqrfWRHWLVTDI--------KGADLKKGKI-QGQEL--------SAYQA 138
Cdd:TIGR00481  16 PPLSWDGVPEGAkSLALTCIDPDAPTGCG-----WWHWVVVNIpadttvlpENASSDDKRLpQGVPLqgrndfgkSGYIG 90

                          90
                  ....*....|....*..
gi 1388875960 139 PSPPahSGFHRYQFFVY 155
Cdd:TIGR00481  91 PCPP--KGDHRYLFTVY 105
PRK09818 PRK09818
kinase inhibitor;
77-174 7.65e-04

kinase inhibitor;


Pssm-ID: 182092  Cd Length: 183  Bit Score: 39.16  E-value: 7.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388875960  77 PIVKFPGAVDGA-TYILVMVDPDAPSRAEprqrfWRHWLVTDI--------------KGADLKKGKIQGQE---LSAYQA 138
Cdd:PRK09818   53 PSLTWSGAPEGTkSFAVTVYDPDAPTGSG-----WWHWTVANIpatvtylpadagrrDGTKLPTGAVQGRNdfgYAGFGG 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1388875960 139 PSPPAHSGFHRYQFFVY-LQEGKvislLPKENKTRGS 174
Cdd:PRK09818  128 ACPPKGDKPHHYQFKVWaLKTDK----IPVDSNSSGA 160
 
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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