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Conserved domains on  [gi|347800659|ref|NP_001009369|]
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large ribosomal subunit protein mL38 [Rattus norvegicus]

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; ...
 171-321 1.34e-43

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: 148.68  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 171 VPLHVAYAlgeeDLIPVYHGNEVTPTEASQAPEVTYEA--DKDSLWTLLFINLDGHLLEPD--AEYLHWLVTNIPSN--- 243
Cdd:cd00866    1 VDLTVSYG----SSGVVTPGNLLTPSETQKAPTVSFSSedPPDKLYTLVMVDPDAPSRDDPkfREWLHWLVTNIPGSdtt 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 244 --RVAEGQESCPYLPPFPARGSGFHRFAFLLFKQDKPINFSEDTRPsPCYQLAQRTFHTLDFYKKHQEAMtPAGLAFFQC 321
Cdd:cd00866   77 tgLVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFPESKLP-PTSGLGRRGFDVREFAKKNGLGL-PVAANFFQV 154
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 171-321 1.34e-43

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: 148.68  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 171 VPLHVAYAlgeeDLIPVYHGNEVTPTEASQAPEVTYEA--DKDSLWTLLFINLDGHLLEPD--AEYLHWLVTNIPSN--- 243
Cdd:cd00866    1 VDLTVSYG----SSGVVTPGNLLTPSETQKAPTVSFSSedPPDKLYTLVMVDPDAPSRDDPkfREWLHWLVTNIPGSdtt 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 244 --RVAEGQESCPYLPPFPARGSGFHRFAFLLFKQDKPINFSEDTRPsPCYQLAQRTFHTLDFYKKHQEAMtPAGLAFFQC 321
Cdd:cd00866   77 tgLVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFPESKLP-PTSGLGRRGFDVREFAKKNGLGL-PVAANFFQV 154
PLN00169 PLN00169
CETS family protein; Provisional
 167-322 2.58e-10

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 59.05  E-value: 2.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 167 FVPWVPLHVAYALGEedlipVYHGNEVTPTEASQAPEVTYEA-DKDSLWTLLfinldghLLEPDA---------EYLHWL 236
Cdd:PLN00169  22 FTRSISLRVTYGSRE-----VNNGCELKPSQVVNQPRVDIGGeDLRTFYTLV-------MVDPDApspsnpnlrEYLHWL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 237 VTNIPSNRVAE-GQESCPYLPPFPArgSGFHRFAFLLFKQdkpinFSEDTRPSPCYqlaQRTFHTLDFYKKHQEAMtPAG 315
Cdd:PLN00169  90 VTDIPATTGATfGQEVVCYESPRPT--AGIHRFVFVLFRQ-----LGRQTVYAPGW---RQNFNTRDFAELYNLGS-PVA 158


                 ....*..
gi 347800659 316 LAFFQCR 322
Cdd:PLN00169 159 AVYFNCQ 165
PBP pfam01161
Phosphatidylethanolamine-binding protein;
185-278 1.65e-09

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 55.81  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659  185 IPV---YHGNEVTPT-EASQAPEVTyeadkDSLwTLLFINLDGHLLePDAEYLHWLVTNIPSNRV--AEGQE-------- 250
Cdd:pfam01161   2 LPVkytCGGPNTSPPlAWSGAPAGT-----KSF-ALVMIDPDAPKV-GGSGWLHWVVTNIPATVTelPEGAPagavqgln 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 347800659  251 ---SCPYLPPFPARGSGFHRFAFLLFKQDKP 278
Cdd:pfam01161  75 dfgGAGYGGPCPPAGDGPHRYVFTLYALDVP 105
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 228-287 6.70e-03

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


Pssm-ID: 441485  Cd Length: 151  Bit Score: 36.67  E-value: 6.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 228 PDA----EYLHWLVTNIPSNR--VAEGQESCP----------------YLPPFPARGSGFHRFAFLLFKQDKPINFSEDT 285
Cdd:COG1881   48 PDAptggGFWHWVVYNIPADVteLPEGAGSADlpagavqgrndfgeagYGGPCPPPGDGPHRYVFTVYALDVELDLPPGA 127


                 ..
gi 347800659 286 RP 287
Cdd:COG1881  128 TR 129
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 171-321 1.34e-43

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: 148.68  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 171 VPLHVAYAlgeeDLIPVYHGNEVTPTEASQAPEVTYEA--DKDSLWTLLFINLDGHLLEPD--AEYLHWLVTNIPSN--- 243
Cdd:cd00866    1 VDLTVSYG----SSGVVTPGNLLTPSETQKAPTVSFSSedPPDKLYTLVMVDPDAPSRDDPkfREWLHWLVTNIPGSdtt 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 244 --RVAEGQESCPYLPPFPARGSGFHRFAFLLFKQDKPINFSEDTRPsPCYQLAQRTFHTLDFYKKHQEAMtPAGLAFFQC 321
Cdd:cd00866   77 tgLVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFPESKLP-PTSGLGRRGFDVREFAKKNGLGL-PVAANFFQV 154
PLN00169 PLN00169
CETS family protein; Provisional
 167-322 2.58e-10

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 59.05  E-value: 2.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 167 FVPWVPLHVAYALGEedlipVYHGNEVTPTEASQAPEVTYEA-DKDSLWTLLfinldghLLEPDA---------EYLHWL 236
Cdd:PLN00169  22 FTRSISLRVTYGSRE-----VNNGCELKPSQVVNQPRVDIGGeDLRTFYTLV-------MVDPDApspsnpnlrEYLHWL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 237 VTNIPSNRVAE-GQESCPYLPPFPArgSGFHRFAFLLFKQdkpinFSEDTRPSPCYqlaQRTFHTLDFYKKHQEAMtPAG 315
Cdd:PLN00169  90 VTDIPATTGATfGQEVVCYESPRPT--AGIHRFVFVLFRQ-----LGRQTVYAPGW---RQNFNTRDFAELYNLGS-PVA 158


                 ....*..
gi 347800659 316 LAFFQCR 322
Cdd:PLN00169 159 AVYFNCQ 165
PBP pfam01161
Phosphatidylethanolamine-binding protein;
185-278 1.65e-09

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 55.81  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659  185 IPV---YHGNEVTPT-EASQAPEVTyeadkDSLwTLLFINLDGHLLePDAEYLHWLVTNIPSNRV--AEGQE-------- 250
Cdd:pfam01161   2 LPVkytCGGPNTSPPlAWSGAPAGT-----KSF-ALVMIDPDAPKV-GGSGWLHWVVTNIPATVTelPEGAPagavqgln 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 347800659  251 ---SCPYLPPFPARGSGFHRFAFLLFKQDKP 278
Cdd:pfam01161  75 dfgGAGYGGPCPPAGDGPHRYVFTLYALDVP 105
PEBP cd00457
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ...
 202-283 2.06e-07

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: 50.09  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 202 PEVTY--EADKDSLWTLLFINLDGHLLEPdaeYLHWLVTNIPSN--------RVAEGQESC---------------PYLP 256
Cdd:cd00457   27 PSLSWdgPPPDVKEYVLVMEDPDAPLGRP---IVHGLVYGIPANktslsnddFVVTDNGKGglqggfkygknrggtVYIG 103

                         90       100
                 ....*....|....*....|....*..
gi 347800659 257 PFPARGSGFHRFAFLLFKQDKPINFSE 283
Cdd:cd00457  104 PRPPLGHGPHRYFFQVYALDEPLDRSK 130
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 228-287 6.70e-03

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


Pssm-ID: 441485  Cd Length: 151  Bit Score: 36.67  E-value: 6.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347800659 228 PDA----EYLHWLVTNIPSNR--VAEGQESCP----------------YLPPFPARGSGFHRFAFLLFKQDKPINFSEDT 285
Cdd:COG1881   48 PDAptggGFWHWVVYNIPADVteLPEGAGSADlpagavqgrndfgeagYGGPCPPPGDGPHRYVFTVYALDVELDLPPGA 127


                 ..
gi 347800659 286 RP 287
Cdd:COG1881  128 TR 129
 
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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