NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16128466|ref|NP_415015|]
View 

TraB family protein YbaP [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

TraB/GumN family protein( domain architecture ID 12999764)

TraB/GumN family protein similar to eukaryotic metalloprotease TIKI, which acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins

EC:  3.4.-.-
Gene Ontology:  GO:0008233
PubMed:  23673329

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Tiki cd14789
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
30-264 1.97e-61

Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is a membrane-associated metalloprotease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In xenopus, tiki is critical in head development. In human cells, TIKI inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of WNT contributes to birth defects, cancer and various diseases. TIKI homology domains are part of the TraB family and are related to the Erythromycin esterase, GumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, Chan-like proteins. TraB/PrgY are identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne, TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to TIKI activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. The TIKI/TraB family has 2 conserved GxxH motifs and conserved glutamate and arginine residues that may be catalytic.


:

Pssm-ID: 350614  Cd Length: 259  Bit Score: 194.44  E-value: 1.97e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466  30 GNRHFHLIGSIHMGSHDMAPLPTRLLKKLKNADALIVEADVSTSDTP------FANLPACEALEERISEEQLQNLQHISQ 103
Cdd:cd14789   7 GGLTSYLFGTIHVGDPDVYPLPPAVEQALAASDALVLELDLTDPAALaalqaaMALPPDGKTLKDLLSPEDYARLKAALA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 104 EMGISPSLFSTQPLWQIAMVLQATQAQKLGLRAEYGIDYQLLQAAKQQHKPVIELEGAENQIAMLLQLPDKG-LALLDDT 182
Cdd:cd14789  87 ELGLPLAALDKLKPWLLALTLSQLQLQKLGYDPEYGVDLYLAQRAKAAGKPVLGLETVEEQLDLLDSLPEEEqLALLRST 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 183 LTHWHTNARLLQQMMSWWLNAPPQ---NNDITLPNTFSQSLYDVLMHQRNLAWRDKLRAM--PPGRYVVAVGALHLYGEG 257
Cdd:cd14789 167 LDELEEAEAELETLIEAWKAGDLDaleELLDESMKEDDPELYERLLVDRNRNWAPKIEALlkKGGTVFVAVGAGHLVGED 246

                ....*..
gi 16128466 258 NLPQMLR 264
Cdd:cd14789 247 GLLALLR 253
 
Name Accession Description Interval E-value
Tiki cd14789
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
30-264 1.97e-61

Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is a membrane-associated metalloprotease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In xenopus, tiki is critical in head development. In human cells, TIKI inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of WNT contributes to birth defects, cancer and various diseases. TIKI homology domains are part of the TraB family and are related to the Erythromycin esterase, GumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, Chan-like proteins. TraB/PrgY are identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne, TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to TIKI activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. The TIKI/TraB family has 2 conserved GxxH motifs and conserved glutamate and arginine residues that may be catalytic.


Pssm-ID: 350614  Cd Length: 259  Bit Score: 194.44  E-value: 1.97e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466  30 GNRHFHLIGSIHMGSHDMAPLPTRLLKKLKNADALIVEADVSTSDTP------FANLPACEALEERISEEQLQNLQHISQ 103
Cdd:cd14789   7 GGLTSYLFGTIHVGDPDVYPLPPAVEQALAASDALVLELDLTDPAALaalqaaMALPPDGKTLKDLLSPEDYARLKAALA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 104 EMGISPSLFSTQPLWQIAMVLQATQAQKLGLRAEYGIDYQLLQAAKQQHKPVIELEGAENQIAMLLQLPDKG-LALLDDT 182
Cdd:cd14789  87 ELGLPLAALDKLKPWLLALTLSQLQLQKLGYDPEYGVDLYLAQRAKAAGKPVLGLETVEEQLDLLDSLPEEEqLALLRST 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 183 LTHWHTNARLLQQMMSWWLNAPPQ---NNDITLPNTFSQSLYDVLMHQRNLAWRDKLRAM--PPGRYVVAVGALHLYGEG 257
Cdd:cd14789 167 LDELEEAEAELETLIEAWKAGDLDaleELLDESMKEDDPELYERLLVDRNRNWAPKIEALlkKGGTVFVAVGAGHLVGED 246

                ....*..
gi 16128466 258 NLPQMLR 264
Cdd:cd14789 247 GLLALLR 253
TraB COG3735
Uncharacterized conserved protein YbaP, TraB family [Function unknown];
30-264 1.28e-54

Uncharacterized conserved protein YbaP, TraB family [Function unknown];


Pssm-ID: 442949  Cd Length: 293  Bit Score: 177.85  E-value: 1.28e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466  30 GNRHFHLIGSIHMGSHDMAPLPTRLLKKLKNADALIVEADVSTSDTPF-------ANLPACEALEERISEEQLQNLQHIS 102
Cdd:COG3735  37 GGKTSYLFGTIHVLDPRDYPLPPAVEEALAAADTLVLELDPDDPDALAlqalmklMLLPDGKTLSDLLSPEEYARLEALL 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 103 QEMGISPSLFSTQPLWQIAMVLQATQAQKLGLRAEYGIDYQLLQAAKQQHKPVIELEGAENQIAMLLQLP-DKGLALLDD 181
Cdd:COG3735 117 AALGLPLAALARLKPWFAALLLSLAALQKAGLDPETGVDMYLLKLAKAAGKPVVGLETVEEQLALLDSLPeEEQAEMLRE 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 182 TLTHWHTNARLLQQMMSWWLNappQNND-----ITLPNTFSQSLYDVLMHQRNLAWRDKLRAMP--PGRYVVAVGALHLY 254
Cdd:COG3735 197 TLDELEKGEAQLETLVDAWRA---GDLAalealLREDMAAYPEFYEALLDDRNRNWAPRIEALLkePGTVFVAVGALHLP 273
                       250
                ....*....|
gi 16128466 255 GEGNLPQMLR 264
Cdd:COG3735 274 GEDGVLALLR 283
TraB_PrgY_gumN pfam01963
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
35-264 1.28e-43

TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora Enterococcusfaecalis and gumN from the plant pathogen Xanthomonas. Tiki1 is homologous to TraB/PrgY. They have a pair of widely spaced GX2H motifs and a conserved glutamate. From the structural study, this group of proteins have been identified as an ancient metalloprotease clan with a common protein architecture (cobbled from the folds of the EreA/ChaN/PMT group) that mediates proteolytic activities. Tiki1 is a membrane-associated protease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. TraB/PrgY is an inhibitor peptide that may act as a protease to inactivate the mating pheromone.


Pssm-ID: 426534  Cd Length: 262  Bit Score: 148.66  E-value: 1.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466    35 HLIGSIHMGSHDMAPLPTRLLKKLKNADALIVEADVSTSDTP--------FANLPACEALEERISEEQLQNLQHISQEMG 106
Cdd:pfam01963  13 YLLGTIHVLPPSVYPLPPAIEEALEAADTVVVELDLSRYTDPatqaalpkLGLLPDGKTLSDLLSPELYARLQKALAKRG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466   107 ISPSLFSTQPLWQIAMVLQATQ--AQKLGLRAEYgIDYQLLQAAKQQHKPVIELEGAENQIAMLLQLPDKGLALLDDTLT 184
Cdd:pfam01963  93 LPLAALDRMKPWLAALLLSLAElaKQKAGLDPDL-VDRYLAKTAKRAGKPVGGLETVEEQLALLSLPDEEQLEMLEETLD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466   185 HWHTNARLLQQMMSWWLNAppQNNDITLPNTFSQS---LYDVLMHQRNLAWRDKLRAM--PPGRYVVAVGALHLYGEGNL 259
Cdd:pfam01963 172 ELEKGEDLLETLVEAWAEG--DLEALELEAELKEAypeLYEVLLDERNRYWAEKIEALlkEGGTVFVAVGAGHLPGEDGV 249

                  ....*
gi 16128466   260 PQMLR 264
Cdd:pfam01963 250 LALLR 254
 
Name Accession Description Interval E-value
Tiki cd14789
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
30-264 1.97e-61

Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is a membrane-associated metalloprotease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In xenopus, tiki is critical in head development. In human cells, TIKI inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of WNT contributes to birth defects, cancer and various diseases. TIKI homology domains are part of the TraB family and are related to the Erythromycin esterase, GumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, Chan-like proteins. TraB/PrgY are identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne, TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to TIKI activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. The TIKI/TraB family has 2 conserved GxxH motifs and conserved glutamate and arginine residues that may be catalytic.


Pssm-ID: 350614  Cd Length: 259  Bit Score: 194.44  E-value: 1.97e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466  30 GNRHFHLIGSIHMGSHDMAPLPTRLLKKLKNADALIVEADVSTSDTP------FANLPACEALEERISEEQLQNLQHISQ 103
Cdd:cd14789   7 GGLTSYLFGTIHVGDPDVYPLPPAVEQALAASDALVLELDLTDPAALaalqaaMALPPDGKTLKDLLSPEDYARLKAALA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 104 EMGISPSLFSTQPLWQIAMVLQATQAQKLGLRAEYGIDYQLLQAAKQQHKPVIELEGAENQIAMLLQLPDKG-LALLDDT 182
Cdd:cd14789  87 ELGLPLAALDKLKPWLLALTLSQLQLQKLGYDPEYGVDLYLAQRAKAAGKPVLGLETVEEQLDLLDSLPEEEqLALLRST 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 183 LTHWHTNARLLQQMMSWWLNAPPQ---NNDITLPNTFSQSLYDVLMHQRNLAWRDKLRAM--PPGRYVVAVGALHLYGEG 257
Cdd:cd14789 167 LDELEEAEAELETLIEAWKAGDLDaleELLDESMKEDDPELYERLLVDRNRNWAPKIEALlkKGGTVFVAVGAGHLVGED 246

                ....*..
gi 16128466 258 NLPQMLR 264
Cdd:cd14789 247 GLLALLR 253
TraB COG3735
Uncharacterized conserved protein YbaP, TraB family [Function unknown];
30-264 1.28e-54

Uncharacterized conserved protein YbaP, TraB family [Function unknown];


Pssm-ID: 442949  Cd Length: 293  Bit Score: 177.85  E-value: 1.28e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466  30 GNRHFHLIGSIHMGSHDMAPLPTRLLKKLKNADALIVEADVSTSDTPF-------ANLPACEALEERISEEQLQNLQHIS 102
Cdd:COG3735  37 GGKTSYLFGTIHVLDPRDYPLPPAVEEALAAADTLVLELDPDDPDALAlqalmklMLLPDGKTLSDLLSPEEYARLEALL 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 103 QEMGISPSLFSTQPLWQIAMVLQATQAQKLGLRAEYGIDYQLLQAAKQQHKPVIELEGAENQIAMLLQLP-DKGLALLDD 181
Cdd:COG3735 117 AALGLPLAALARLKPWFAALLLSLAALQKAGLDPETGVDMYLLKLAKAAGKPVVGLETVEEQLALLDSLPeEEQAEMLRE 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466 182 TLTHWHTNARLLQQMMSWWLNappQNND-----ITLPNTFSQSLYDVLMHQRNLAWRDKLRAMP--PGRYVVAVGALHLY 254
Cdd:COG3735 197 TLDELEKGEAQLETLVDAWRA---GDLAalealLREDMAAYPEFYEALLDDRNRNWAPRIEALLkePGTVFVAVGALHLP 273
                       250
                ....*....|
gi 16128466 255 GEGNLPQMLR 264
Cdd:COG3735 274 GEDGVLALLR 283
TraB_PrgY_gumN pfam01963
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
35-264 1.28e-43

TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora Enterococcusfaecalis and gumN from the plant pathogen Xanthomonas. Tiki1 is homologous to TraB/PrgY. They have a pair of widely spaced GX2H motifs and a conserved glutamate. From the structural study, this group of proteins have been identified as an ancient metalloprotease clan with a common protein architecture (cobbled from the folds of the EreA/ChaN/PMT group) that mediates proteolytic activities. Tiki1 is a membrane-associated protease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. TraB/PrgY is an inhibitor peptide that may act as a protease to inactivate the mating pheromone.


Pssm-ID: 426534  Cd Length: 262  Bit Score: 148.66  E-value: 1.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466    35 HLIGSIHMGSHDMAPLPTRLLKKLKNADALIVEADVSTSDTP--------FANLPACEALEERISEEQLQNLQHISQEMG 106
Cdd:pfam01963  13 YLLGTIHVLPPSVYPLPPAIEEALEAADTVVVELDLSRYTDPatqaalpkLGLLPDGKTLSDLLSPELYARLQKALAKRG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466   107 ISPSLFSTQPLWQIAMVLQATQ--AQKLGLRAEYgIDYQLLQAAKQQHKPVIELEGAENQIAMLLQLPDKGLALLDDTLT 184
Cdd:pfam01963  93 LPLAALDRMKPWLAALLLSLAElaKQKAGLDPDL-VDRYLAKTAKRAGKPVGGLETVEEQLALLSLPDEEQLEMLEETLD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466   185 HWHTNARLLQQMMSWWLNAppQNNDITLPNTFSQS---LYDVLMHQRNLAWRDKLRAM--PPGRYVVAVGALHLYGEGNL 259
Cdd:pfam01963 172 ELEKGEDLLETLVEAWAEG--DLEALELEAELKEAypeLYEVLLDERNRYWAEKIEALlkEGGTVFVAVGAGHLPGEDGV 249

                  ....*
gi 16128466   260 PQMLR 264
Cdd:pfam01963 250 LALLR 254
MopB_Thiosulfate-R-like cd02755
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ...
48-134 3.27e-03

The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239156 [Multi-domain]  Cd Length: 454  Bit Score: 38.43  E-value: 3.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128466  48 APLPTRLLKKLKNADaLIVEADVSTSDTP-FAN--LPACEALEErisEEQLQNLQHISQEMGIS----PSLFSTQPLWQI 120
Cdd:cd02755 345 MPDRARLIKALKNLD-LVVAIDILPSDTAlYADviLPEATYLER---DEPFSDKGGPAPAVATRqraiEPLYDTRPGWDI 420
                        90
                ....*....|....
gi 16128466 121 AMVLqatqAQKLGL 134
Cdd:cd02755 421 LKEL----ARRLGL 430
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH