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Conserved domains on  [gi|169636418|ref|NP_115867|]
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large ribosomal subunit protein mL38 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; ...
 171-321 1.40e-36

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: 130.19  E-value: 1.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 171 VPLHVAYavgeDDLMPVYCGNEVTPTEAAQAPEVTYEAEEGSlwtllltslDGH----LLEPDA---------EYLHWLL 237
Cdd:cd00866    1 VDLTVSY----GSSGVVTPGNLLTPSETQKAPTVSFSSEDPP---------DKLytlvMVDPDApsrddpkfrEWLHWLV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 238 TNIPGN-----RVAEGQVTCPYLPPFPARGSGIHRLAFLLFKQDQPIDFSEDARPsPCYQLAQRTFRTFDFYKKHQETMt 312
Cdd:cd00866   68 TNIPGSdtttgLVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFPESKLP-PTSGLGRRGFDVREFAKKNGLGL- 145


                 ....*....
gi 169636418 313 PAGLSFFQC 321
Cdd:cd00866  146 PVAANFFQV 154
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 171-321 1.40e-36

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: 130.19  E-value: 1.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 171 VPLHVAYavgeDDLMPVYCGNEVTPTEAAQAPEVTYEAEEGSlwtllltslDGH----LLEPDA---------EYLHWLL 237
Cdd:cd00866    1 VDLTVSY----GSSGVVTPGNLLTPSETQKAPTVSFSSEDPP---------DKLytlvMVDPDApsrddpkfrEWLHWLV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 238 TNIPGN-----RVAEGQVTCPYLPPFPARGSGIHRLAFLLFKQDQPIDFSEDARPsPCYQLAQRTFRTFDFYKKHQETMt 312
Cdd:cd00866   68 TNIPGSdtttgLVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFPESKLP-PTSGLGRRGFDVREFAKKNGLGL- 145


                 ....*....
gi 169636418 313 PAGLSFFQC 321
Cdd:cd00866  146 PVAANFFQV 154
PBP pfam01161
Phosphatidylethanolamine-binding protein;
228-278 5.06e-08

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 51.19  E-value: 5.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418  228 PDA------EYLHWLLTNIPGNRV--AEGQV-----------TCPYLPPFPARGSGIHRLAFLLFKQDQP 278
Cdd:pfam01161  36 PDApkvggsGWLHWVVTNIPATVTelPEGAPagavqglndfgGAGYGGPCPPAGDGPHRYVFTLYALDVP 105
PLN00169 PLN00169
CETS family protein; Provisional
 167-275 1.34e-07

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 50.96  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 167 FVPRVPLHVAYAVGEddlmpVYCGNEVTPTEAAQAPEVTYEAEEGSLWTLLLtsldghLLEPDA---------EYLHWLL 237
Cdd:PLN00169  22 FTRSISLRVTYGSRE-----VNNGCELKPSQVVNQPRVDIGGEDLRTFYTLV------MVDPDApspsnpnlrEYLHWLV 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 169636418 238 TNIPGNRVAE-GQVTCPYLPPFPArgSGIHRLAFLLFKQ 275
Cdd:PLN00169  91 TDIPATTGATfGQEVVCYESPRPT--AGIHRFVFVLFRQ 127
 
Name Accession Description Interval E-value
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 171-321 1.40e-36

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: 130.19  E-value: 1.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 171 VPLHVAYavgeDDLMPVYCGNEVTPTEAAQAPEVTYEAEEGSlwtllltslDGH----LLEPDA---------EYLHWLL 237
Cdd:cd00866    1 VDLTVSY----GSSGVVTPGNLLTPSETQKAPTVSFSSEDPP---------DKLytlvMVDPDApsrddpkfrEWLHWLV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 238 TNIPGN-----RVAEGQVTCPYLPPFPARGSGIHRLAFLLFKQDQPIDFSEDARPsPCYQLAQRTFRTFDFYKKHQETMt 312
Cdd:cd00866   68 TNIPGSdtttgLVSKGEVLVPYLGPGPPKGTGPHRYVFLLFKQPGGLDFPESKLP-PTSGLGRRGFDVREFAKKNGLGL- 145


                 ....*....
gi 169636418 313 PAGLSFFQC 321
Cdd:cd00866  146 PVAANFFQV 154
PBP pfam01161
Phosphatidylethanolamine-binding protein;
228-278 5.06e-08

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 51.19  E-value: 5.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418  228 PDA------EYLHWLLTNIPGNRV--AEGQV-----------TCPYLPPFPARGSGIHRLAFLLFKQDQP 278
Cdd:pfam01161  36 PDApkvggsGWLHWVVTNIPATVTelPEGAPagavqglndfgGAGYGGPCPPAGDGPHRYVFTLYALDVP 105
PLN00169 PLN00169
CETS family protein; Provisional
 167-275 1.34e-07

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 50.96  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 167 FVPRVPLHVAYAVGEddlmpVYCGNEVTPTEAAQAPEVTYEAEEGSLWTLLLtsldghLLEPDA---------EYLHWLL 237
Cdd:PLN00169  22 FTRSISLRVTYGSRE-----VNNGCELKPSQVVNQPRVDIGGEDLRTFYTLV------MVDPDApspsnpnlrEYLHWLV 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 169636418 238 TNIPGNRVAE-GQVTCPYLPPFPArgSGIHRLAFLLFKQ 275
Cdd:PLN00169  91 TDIPATTGATfGQEVVCYESPRPT--AGIHRFVFVLFRQ 127
PEBP cd00457
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ...
 228-283 9.25e-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: 48.16  E-value: 9.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636418 228 PDA----EYLHWLLTNIPGNRVAEGQV-----------------------TCPYLPPFPARGSGIHRLAFLLFKQDQPID 280
Cdd:cd00457   48 PDAplgrPIVHGLVYGIPANKTSLSNDdfvvtdngkgglqggfkygknrgGTVYIGPRPPLGHGPHRYFFQVYALDEPLD 127


                 ...
gi 169636418 281 FSE 283
Cdd:cd00457  128 RSK 130
 
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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