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Conserved domains on  [gi|565373402|ref|XP_006353263|]
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PREDICTED: protein FLOWERING LOCUS T-like [Solanum tuberosum]

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 ...
 1-173 2.26e-110

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: 311.74  E-value: 2.26e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402   1 MQRERDTLTLARVIGDVLDPFTRSINLRVVYNNREVRNGCDLRPSMVINQPSVEIEGDNLQTFYTLVMVDPDAPTPSNPY 80
Cdd:PLN00169   2 SPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNPN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402  81 HKEYLHWLVTDIPASTGVTFGNEVVSYECPRPTMGIHRLVLVLFRQLRREIVHAPENRQNFDTRDFAKVYNFGLPVAAVY 160
Cdd:PLN00169  82 LREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDFAELYNLGSPVAAVY 161

                        170
                 ....*....|...
gi 565373402 161 FNCQRENGTGGRR 173
Cdd:PLN00169 162 FNCQRESGSGGRR 174
 
Name Accession Description Interval E-value
PLN00169 PLN00169
CETS family protein; Provisional
 1-173 2.26e-110

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 311.74  E-value: 2.26e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402   1 MQRERDTLTLARVIGDVLDPFTRSINLRVVYNNREVRNGCDLRPSMVINQPSVEIEGDNLQTFYTLVMVDPDAPTPSNPY 80
Cdd:PLN00169   2 SPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNPN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402  81 HKEYLHWLVTDIPASTGVTFGNEVVSYECPRPTMGIHRLVLVLFRQLRREIVHAPENRQNFDTRDFAKVYNFGLPVAAVY 160
Cdd:PLN00169  82 LREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDFAELYNLGSPVAAVY 161

                        170
                 ....*....|...
gi 565373402 161 FNCQRENGTGGRR 173
Cdd:PLN00169 162 FNCQRESGSGGRR 174
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 26-163 3.05e-45

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: 145.98  E-value: 3.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402  26 NLRVVYNN-REVRNGCDLRPSMVINQPSVEIEG-DNLQTFYTLVMVDPDAPTPSNPYHKEYLHWLVTDIPASTG----VT 99
Cdd:cd00866    2 DLTVSYGSsGVVTPGNLLTPSETQKAPTVSFSSeDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTttglVS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565373402 100 FGNEVVSYECPRPTM--GIHRLVLVLFRQ-------LRREIVHAPENRQNFDTRDFAKVYNFGLPVAAVYFNC 163
Cdd:cd00866   82 KGEVLVPYLGPGPPKgtGPHRYVFLLFKQpggldfpESKLPPTSGLGRRGFDVREFAKKNGLGLPVAANFFQV 154
PBP pfam01161
Phosphatidylethanolamine-binding protein;
50-126 1.67e-11

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 58.51  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402   50 QPSVEIEGDNLQT-FYTLVMVDPDAPTPSnpyHKEYLHWLVTDIPAST-----GVTFG-----NEVVSYE----CPRPTM 114
Cdd:pfam01161  14 SPPLAWSGAPAGTkSFALVMIDPDAPKVG---GSGWLHWVVTNIPATVtelpeGAPAGavqglNDFGGAGyggpCPPAGD 90

                          90
                  ....*....|..
gi 565373402  115 GIHRLVLVLFRQ 126
Cdd:pfam01161  91 GPHRYVFTLYAL 102
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 64-124 1.98e-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: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402  64 YTLVMVDPDAPTPSNpyhkeYLHWLVTDIPAST------------------GVT-FGNevVSYE--CPRPTMGIHRLVLV 122
Cdd:COG1881   41 FALIVEDPDAPTGGG-----FWHWVVYNIPADVtelpegagsadlpagavqGRNdFGE--AGYGgpCPPPGDGPHRYVFT 113


                 ..
gi 565373402 123 LF 124
Cdd:COG1881  114 VY 115
 
Name Accession Description Interval E-value
PLN00169 PLN00169
CETS family protein; Provisional
 1-173 2.26e-110

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 311.74  E-value: 2.26e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402   1 MQRERDTLTLARVIGDVLDPFTRSINLRVVYNNREVRNGCDLRPSMVINQPSVEIEGDNLQTFYTLVMVDPDAPTPSNPY 80
Cdd:PLN00169   2 SPRDRDPLVVGRVVGDVLDPFTRSISLRVTYGSREVNNGCELKPSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNPN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402  81 HKEYLHWLVTDIPASTGVTFGNEVVSYECPRPTMGIHRLVLVLFRQLRREIVHAPENRQNFDTRDFAKVYNFGLPVAAVY 160
Cdd:PLN00169  82 LREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDFAELYNLGSPVAAVY 161

                        170
                 ....*....|...
gi 565373402 161 FNCQRENGTGGRR 173
Cdd:PLN00169 162 FNCQRESGSGGRR 174
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 26-163 3.05e-45

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: 145.98  E-value: 3.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402  26 NLRVVYNN-REVRNGCDLRPSMVINQPSVEIEG-DNLQTFYTLVMVDPDAPTPSNPYHKEYLHWLVTDIPASTG----VT 99
Cdd:cd00866    2 DLTVSYGSsGVVTPGNLLTPSETQKAPTVSFSSeDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTttglVS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565373402 100 FGNEVVSYECPRPTM--GIHRLVLVLFRQ-------LRREIVHAPENRQNFDTRDFAKVYNFGLPVAAVYFNC 163
Cdd:cd00866   82 KGEVLVPYLGPGPPKgtGPHRYVFLLFKQpggldfpESKLPPTSGLGRRGFDVREFAKKNGLGLPVAANFFQV 154
PEBP cd00457
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ...
 39-163 2.41e-14

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: 66.65  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402  39 GCDLRPSmvINQPSVEIEGDnlqtFYTLVMVDPDAPTPSnpyhkEYLHWLVTDIPAS-TGVTFGNEVVS----------- 106
Cdd:cd00457   22 GVGRFPS--LSWDGPPPDVK----EYVLVMEDPDAPLGR-----PIVHGLVYGIPANkTSLSNDDFVVTdngkgglqggf 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402 107 ----------YECPRPTM--GIHRLVLVLFRQL-RREIVHAPENRQNFDTRDFAKVYNFGlPVAAVYFNC 163
Cdd:cd00457   91 kygknrggtvYIGPRPPLghGPHRYFFQVYALDePLDRSKLGDGRTKFEVARFAEGNVLG-AVGEWVGQF 159
PBP pfam01161
Phosphatidylethanolamine-binding protein;
50-126 1.67e-11

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 58.51  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402   50 QPSVEIEGDNLQT-FYTLVMVDPDAPTPSnpyHKEYLHWLVTDIPAST-----GVTFG-----NEVVSYE----CPRPTM 114
Cdd:pfam01161  14 SPPLAWSGAPAGTkSFALVMIDPDAPKVG---GSGWLHWVVTNIPATVtelpeGAPAGavqglNDFGGAGyggpCPPAGD 90

                          90
                  ....*....|..
gi 565373402  115 GIHRLVLVLFRQ 126
Cdd:pfam01161  91 GPHRYVFTLYAL 102
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 64-124 1.98e-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: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565373402  64 YTLVMVDPDAPTPSNpyhkeYLHWLVTDIPAST------------------GVT-FGNevVSYE--CPRPTMGIHRLVLV 122
Cdd:COG1881   41 FALIVEDPDAPTGGG-----FWHWVVYNIPADVtelpegagsadlpagavqGRNdFGE--AGYGgpCPPPGDGPHRYVFT 113


                 ..
gi 565373402 123 LF 124
Cdd:COG1881  114 VY 115
PEBP_bact_arch cd00865
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea; ...
 64-97 1.32e-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: 42.97  E-value: 1.32e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 565373402  64 YTLVMVDPDAPTPSnpyhkEYLHWLVTDIPASTG 97
Cdd:cd00865   42 LALIVEDPDAPTGG-----GFVHWVVWNIPADTT 70
 
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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