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Conserved domains on  [gi|1479551937|gb|AYA59316|]
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ZCN8, partial [Zea mays subsp. mays]

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 ...
 1-106 4.56e-58

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: 176.54  E-value: 4.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1479551937   1 VLIDPDAPSPSHPSLREYLHWMVTDIPETTSVNFGQELIFYERPDPRSGIHRLVFVLFRQLGRGTVFAPEMRHNFNCRSF 80
Cdd:PLN00169   68 VMVDPDAPSPSNPNLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDF 147

                          90       100
                  ....*....|....*....|....*..
gi 1479551937  81 ARQYHLSIATAT-YFNCQREGGSGGRR 106
Cdd:PLN00169  148 AELYNLGSPVAAvYFNCQRESGSGGRR 174
 
Name Accession Description Interval E-value
PLN00169 PLN00169
CETS family protein; Provisional
 1-106 4.56e-58

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 176.54  E-value: 4.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1479551937   1 VLIDPDAPSPSHPSLREYLHWMVTDIPETTSVNFGQELIFYERPDPRSGIHRLVFVLFRQLGRGTVFAPEMRHNFNCRSF 80
Cdd:PLN00169   68 VMVDPDAPSPSNPNLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDF 147

                          90       100
                  ....*....|....*....|....*..
gi 1479551937  81 ARQYHLSIATAT-YFNCQREGGSGGRR 106
Cdd:PLN00169  148 AELYNLGSPVAAvYFNCQRESGSGGRR 174
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 1-96 7.06e-28

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: 99.37  E-value: 7.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1479551937   1 VLIDPDAPSPSHPSLREYLHWMVTDIP----ETTSVNFGQELIFYERPDP--RSGIHRLVFVLFRQLGRGTVFAPEM--- 71
Cdd:cd00866    45 VMVDPDAPSRDDPKFREWLHWLVTNIPgsdtTTGLVSKGEVLVPYLGPGPpkGTGPHRYVFLLFKQPGGLDFPESKLppt 124

                          90       100       110
                  ....*....|....*....|....*....|
gi 1479551937  72 ----RHNFNCRSFARQYHLSI-ATATYFNC 96
Cdd:cd00866   125 sglgRRGFDVREFAKKNGLGLpVAANFFQV 154
PBP pfam01161
Phosphatidylethanolamine-binding protein;
1-60 4.62e-09

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 50.42  E-value: 4.62e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1479551937   1 VLIDPDAPSPSHPSlreYLHWMVTDIP-ETTSVNFGQELIF-----------YERPDP--RSGIHRLVFVLFRQ 60
Cdd:pfam01161  32 VMIDPDAPKVGGSG---WLHWVVTNIPaTVTELPEGAPAGAvqglndfggagYGGPCPpaGDGPHRYVFTLYAL 102
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 1-58 1.47e-03

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


Pssm-ID: 441485  Cd Length: 151  Bit Score: 35.90  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1479551937   1 VLIDPDAPSPShpslrEYLHWMVTDIP-ETTS-----------------VN-FGQelIFYERPDPRSG--IHRLVFVLF 58
Cdd:COG1881    44 IVEDPDAPTGG-----GFWHWVVYNIPaDVTElpegagsadlpagavqgRNdFGE--AGYGGPCPPPGdgPHRYVFTVY 115
TIGR00481 TIGR00481
Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General]
 2-58 2.86e-03

Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General]


Pssm-ID: 129572  Cd Length: 141  Bit Score: 35.15  E-value: 2.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1479551937   2 LIDPDAPSPShpslrEYLHWMVTDIPETTSV---NFGQELIF-----------------YERPDPRSGIHRLVFVLF 58
Cdd:TIGR00481  34 CIDPDAPTGC-----GWWHWVVVNIPADTTVlpeNASSDDKRlpqgvplqgrndfgksgYIGPCPPKGDHRYLFTVY 105
 
Name Accession Description Interval E-value
PLN00169 PLN00169
CETS family protein; Provisional
 1-106 4.56e-58

CETS family protein; Provisional


Pssm-ID: 177765  Cd Length: 175  Bit Score: 176.54  E-value: 4.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1479551937   1 VLIDPDAPSPSHPSLREYLHWMVTDIPETTSVNFGQELIFYERPDPRSGIHRLVFVLFRQLGRGTVFAPEMRHNFNCRSF 80
Cdd:PLN00169   68 VMVDPDAPSPSNPNLREYLHWLVTDIPATTGATFGQEVVCYESPRPTAGIHRFVFVLFRQLGRQTVYAPGWRQNFNTRDF 147

                          90       100
                  ....*....|....*....|....*..
gi 1479551937  81 ARQYHLSIATAT-YFNCQREGGSGGRR 106
Cdd:PLN00169  148 AELYNLGSPVAAvYFNCQRESGSGGRR 174
PEBP_euk cd00866
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in eukaryotes; ...
 1-96 7.06e-28

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: 99.37  E-value: 7.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1479551937   1 VLIDPDAPSPSHPSLREYLHWMVTDIP----ETTSVNFGQELIFYERPDP--RSGIHRLVFVLFRQLGRGTVFAPEM--- 71
Cdd:cd00866    45 VMVDPDAPSRDDPKFREWLHWLVTNIPgsdtTTGLVSKGEVLVPYLGPGPpkGTGPHRYVFLLFKQPGGLDFPESKLppt 124

                          90       100       110
                  ....*....|....*....|....*....|
gi 1479551937  72 ----RHNFNCRSFARQYHLSI-ATATYFNC 96
Cdd:cd00866   125 sglgRRGFDVREFAKKNGLGLpVAANFFQV 154
PBP pfam01161
Phosphatidylethanolamine-binding protein;
1-60 4.62e-09

Phosphatidylethanolamine-binding protein;


Pssm-ID: 460090  Cd Length: 136  Bit Score: 50.42  E-value: 4.62e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1479551937   1 VLIDPDAPSPSHPSlreYLHWMVTDIP-ETTSVNFGQELIF-----------YERPDP--RSGIHRLVFVLFRQ 60
Cdd:pfam01161  32 VMIDPDAPKVGGSG---WLHWVVTNIPaTVTELPEGAPAGAvqglndfggagYGGPCPpaGDGPHRYVFTLYAL 102
PEBP cd00457
PhosphatidylEthanolamine-Binding Protein (PEBP) domain; PhosphatidylEthanolamine-Binding ...
 1-96 2.20e-08

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: 48.93  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1479551937   1 VLIDPDAPSPshpslREYLHWMVTDIP-ETTSVN-----------FGQELIF----------YERPDP--RSGIHRLVFV 56
Cdd:cd00457    44 VMEDPDAPLG-----RPIVHGLVYGIPaNKTSLSnddfvvtdngkGGLQGGFkygknrggtvYIGPRPplGHGPHRYFFQ 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1479551937  57 LFRQLGRGTVFAP-EMRHNFNCRSFARQYHLSIATATYFNC 96
Cdd:cd00457   119 VYALDEPLDRSKLgDGRTKFEVARFAEGNVLGAVGEWVGQF 159
PEBP COG1881
Uncharacterized conserved protein, phosphatidylethanolamine-binding protein (PEBP) family ...
 1-58 1.47e-03

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


Pssm-ID: 441485  Cd Length: 151  Bit Score: 35.90  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1479551937   1 VLIDPDAPSPShpslrEYLHWMVTDIP-ETTS-----------------VN-FGQelIFYERPDPRSG--IHRLVFVLF 58
Cdd:COG1881    44 IVEDPDAPTGG-----GFWHWVVYNIPaDVTElpegagsadlpagavqgRNdFGE--AGYGGPCPPPGdgPHRYVFTVY 115
PEBP_bact_arch cd00865
PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea; ...
 1-58 2.31e-03

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: 35.27  E-value: 2.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1479551937   1 VLIDPDAPSPShpslrEYLHWMVTDIPETTSV---NFGQEL--------------IFYERPDP-RSGIHRLVFVLF 58
Cdd:cd00865    45 IVEDPDAPTGG-----GFVHWVVWNIPADTTElpeGASRGAlpagavqgrndfgeAGYGGPCPpDGGPHRYVFTVY 115
TIGR00481 TIGR00481
Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General]
 2-58 2.86e-03

Raf kinase inhibitor-like protein, YbhB/YbcL family; [Unknown function, General]


Pssm-ID: 129572  Cd Length: 141  Bit Score: 35.15  E-value: 2.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1479551937   2 LIDPDAPSPShpslrEYLHWMVTDIPETTSV---NFGQELIF-----------------YERPDPRSGIHRLVFVLF 58
Cdd:TIGR00481  34 CIDPDAPTGC-----GWWHWVVVNIPADTTVlpeNASSDDKRlpqgvplqgrndfgksgYIGPCPPKGDHRYLFTVY 105
 
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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