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Conserved domains on  [gi|1246741877|ref|NP_001342831|]
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mitochondrial ribosomal protein subunit L35 [Schizosaccharomyces pombe]

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; ...
 130-279 2.88e-34

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: 122.48  E-value: 2.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246741877 130 VDVQLGFNpeNNDSITPGTILPSTVTVKTPWLSVLPFNCKKNHYSVITLDLDVPNYETNRFETHCNWLLTNIPIEASKRV 209
Cdd:cd00866     1 VDLTVSYG--SSGVVTPGNLLTPSETQKAPTVSFSSEDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTTTG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246741877 210 PIDTSKAFFQYRPPIVHRGEDKHRILTLVLRQK-----SSSISIPSNALVRERFDLSEFCSIYDLE-PVGAHLWRS 279
Cdd:cd00866    79 LVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPggldfPESKLPPTSGLGRRGFDVREFAKKNGLGlPVAANFFQV 154
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 130-279 2.88e-34

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: 122.48  E-value: 2.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246741877 130 VDVQLGFNpeNNDSITPGTILPSTVTVKTPWLSVLPFNCKKNHYSVITLDLDVPNYETNRFETHCNWLLTNIPIEASKRV 209
Cdd:cd00866     1 VDLTVSYG--SSGVVTPGNLLTPSETQKAPTVSFSSEDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTTTG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246741877 210 PIDTSKAFFQYRPPIVHRGEDKHRILTLVLRQK-----SSSISIPSNALVRERFDLSEFCSIYDLE-PVGAHLWRS 279
Cdd:cd00866    79 LVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPggldfPESKLPPTSGLGRRGFDVREFAKKNGLGlPVAANFFQV 154
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 130-279 2.88e-34

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: 122.48  E-value: 2.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246741877 130 VDVQLGFNpeNNDSITPGTILPSTVTVKTPWLSVLPFNCKKNHYSVITLDLDVPNYETNRFETHCNWLLTNIPIEASKRV 209
Cdd:cd00866     1 VDLTVSYG--SSGVVTPGNLLTPSETQKAPTVSFSSEDPPDKLYTLVMVDPDAPSRDDPKFREWLHWLVTNIPGSDTTTG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246741877 210 PIDTSKAFFQYRPPIVHRGEDKHRILTLVLRQK-----SSSISIPSNALVRERFDLSEFCSIYDLE-PVGAHLWRS 279
Cdd:cd00866    79 LVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPggldfPESKLPPTSGLGRRGFDVREFAKKNGLGlPVAANFFQV 154
 
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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