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Conserved domains on  [gi|954489864|gb|KRZ19464|]
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Uncharacterized protein T11_6631, partial [Trichinella zimbabwensis]

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; ...
 413-539 1.08e-18

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: 83.19  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954489864 413 SNPDDAPLYTLLMLDVDASDKMGSASRPYVIWLVTNFAISShlNNALTGSMETTVFSYSRPLP-VGKQLHRYYFLLFQQN 491
Cdd:cd00866   34 SEDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSD--TTTGLVSKGEVLVPYLGPGPpKGTGPHRYVFLLFKQP 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 954489864 492 DGSIthikpeLYSSESCPTEYNGRCFFDVREFMAHHSLTLK-GVSWMRS 539
Cdd:cd00866  112 GGLD------FPESKLPPTSGLGRRGFDVREFAKKNGLGLPvAANFFQV 154
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 413-539 1.08e-18

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: 83.19  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954489864 413 SNPDDAPLYTLLMLDVDASDKMGSASRPYVIWLVTNFAISShlNNALTGSMETTVFSYSRPLP-VGKQLHRYYFLLFQQN 491
Cdd:cd00866   34 SEDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSD--TTTGLVSKGEVLVPYLGPGPpKGTGPHRYVFLLFKQP 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 954489864 492 DGSIthikpeLYSSESCPTEYNGRCFFDVREFMAHHSLTLK-GVSWMRS 539
Cdd:cd00866  112 GGLD------FPESKLPPTSGLGRRGFDVREFAKKNGLGLPvAANFFQV 154
PBP pfam01161
Phosphatidylethanolamine-binding protein;
414-491 1.64e-05

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 45.02  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954489864  414 NPDDAPLYTLLMLDVDASDKMGSasrPYVIWLVTNFAISSHLNN------ALTGSMETTVFSYSRPLP-VGKQLHRYYFL 486
Cdd:pfam01161  22 APAGTKSFALVMIDPDAPKVGGS---GWLHWVVTNIPATVTELPegapagAVQGLNDFGGAGYGGPCPpAGDGPHRYVFT 98


                  ....*
gi 954489864  487 LFQQN 491
Cdd:pfam01161  99 LYALD 103
PLN00169 PLN00169
CETS family protein; Provisional
 372-490 6.92e-05

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 44.03  E-value: 6.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954489864 372 DPL------GDAeIDPVYLRQSPSISVSNYFLNTDL----SHLHYHSPYDYSNPDDAPLYTLLMLDVDASDKMGSASRPY 441
Cdd:PLN00169   7 DPLvvgrvvGDV-LDPFTRSISLRVTYGSREVNNGCelkpSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNPNLREY 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 954489864 442 VIWLVTNFAisshlnnALTG-SMETTVFSYSRPLPVGKqLHRYYFLLFQQ 490
Cdd:PLN00169  86 LHWLVTDIP-------ATTGaTFGQEVVCYESPRPTAG-IHRFVFVLFRQ 127
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 413-539 1.08e-18

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: 83.19  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954489864 413 SNPDDAPLYTLLMLDVDASDKMGSASRPYVIWLVTNFAISShlNNALTGSMETTVFSYSRPLP-VGKQLHRYYFLLFQQN 491
Cdd:cd00866   34 SEDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSD--TTTGLVSKGEVLVPYLGPGPpKGTGPHRYVFLLFKQP 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 954489864 492 DGSIthikpeLYSSESCPTEYNGRCFFDVREFMAHHSLTLK-GVSWMRS 539
Cdd:cd00866  112 GGLD------FPESKLPPTSGLGRRGFDVREFAKKNGLGLPvAANFFQV 154
PBP pfam01161
Phosphatidylethanolamine-binding protein;
414-491 1.64e-05

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 45.02  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954489864  414 NPDDAPLYTLLMLDVDASDKMGSasrPYVIWLVTNFAISSHLNN------ALTGSMETTVFSYSRPLP-VGKQLHRYYFL 486
Cdd:pfam01161  22 APAGTKSFALVMIDPDAPKVGGS---GWLHWVVTNIPATVTELPegapagAVQGLNDFGGAGYGGPCPpAGDGPHRYVFT 98


                  ....*
gi 954489864  487 LFQQN 491
Cdd:pfam01161  99 LYALD 103
PLN00169 PLN00169
CETS family protein; Provisional
 372-490 6.92e-05

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 44.03  E-value: 6.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954489864 372 DPL------GDAeIDPVYLRQSPSISVSNYFLNTDL----SHLHYHSPYDYSNPDDAPLYTLLMLDVDASDKMGSASRPY 441
Cdd:PLN00169   7 DPLvvgrvvGDV-LDPFTRSISLRVTYGSREVNNGCelkpSQVVNQPRVDIGGEDLRTFYTLVMVDPDAPSPSNPNLREY 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 954489864 442 VIWLVTNFAisshlnnALTG-SMETTVFSYSRPLPVGKqLHRYYFLLFQQ 490
Cdd:PLN00169  86 LHWLVTDIP-------ATTGaTFGQEVVCYESPRPTAG-IHRFVFVLFRQ 127
PEBP cd00457
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ...
 413-491 7.50e-03

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: 37.76  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954489864 413 SNPDDAPLYTLLMLDVDASDkmgsaSRPYVIWLVTN----------------FAISSHL--NNALTGSMETTVFSYSRPl 474
Cdd:cd00457   33 GPPPDVKEYVLVMEDPDAPL-----GRPIVHGLVYGipanktslsnddfvvtDNGKGGLqgGFKYGKNRGGTVYIGPRP- 106

                         90
                 ....*....|....*..
gi 954489864 475 PVGKQLHRYYFLLFQQN 491
Cdd:cd00457  107 PLGHGPHRYFFQVYALD 123
 
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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