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Conserved domains on  [gi|1721658289|gb|QEC66710|]
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TraB/GumN family protein [Panacibacter ginsenosidivorans]

Protein Classification

TraB/GumN family protein( domain architecture ID 10007931)

TraB/GumN family protein similar to Escherichia coli protein YbaP and 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TraB COG3735
Uncharacterized conserved protein YbaP, TraB family [Function unknown];
1-310 6.92e-53

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


:

Pssm-ID: 442949  Cd Length: 293  Bit Score: 187.48  E-value: 6.92e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289    1 MKMKIVFVLLSISVVLFAnpfksfsqkkntdsksnTAAANQKKYPSLLWEITGNGlvKPSYLFGTMHISNKMVFNLSDSF 80
Cdd:COG3735      1 MRRRLLLLLLAALLLLAL-----------------AAAAAAAQAGPLLWKVSKGG--KTSYLFGTIHVLDPRDYPLPPAV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289   81 YKAIKSVDVVALEQNPEVWQEAYSREDFNGGNDFIHSQLfrsfnmsNERLTEQTF-SLSNYESKIQLGLASEARM----V 155
Cdd:COG3735     62 EEALAAADTLVLELDPDDPDALALQALMKLMLLPDGKTL-------SDLLSPEEYaRLEALLAALGLPLAALARLkpwfA 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  156 NGMLYRNNVGQEDFEEETYLDMYIYRLGRKLNKIVTGVEDYKES----DKLVKEAYRDMYKD-----KKPRRSYDisgfd 226
Cdd:COG3735    135 ALLLSLAALQKAGLDPETGVDMYLLKLAKAAGKPVVGLETVEEQlallDSLPEEEQAEMLREtldelEKGEAQLE----- 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  227 ykhKMEDAYRKG-DLDLLDSLQDITTVSDAFNEKFLFRRNDIQANSIDTILKKH-SLFVGVGAAHLPGERGVIELLRKKG 304
Cdd:COG3735    210 ---TLVDAWRAGdLAALEALLREDMAAYPEFYEALLDDRNRNWAPRIEALLKEPgTVFVAVGALHLPGEDGVLALLRARG 286

                   ....*.
gi 1721658289  305 YTVRPV 310
Cdd:COG3735    287 YTVERV 292
 
Name Accession Description Interval E-value
TraB COG3735
Uncharacterized conserved protein YbaP, TraB family [Function unknown];
1-310 6.92e-53

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


Pssm-ID: 442949  Cd Length: 293  Bit Score: 187.48  E-value: 6.92e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289    1 MKMKIVFVLLSISVVLFAnpfksfsqkkntdsksnTAAANQKKYPSLLWEITGNGlvKPSYLFGTMHISNKMVFNLSDSF 80
Cdd:COG3735      1 MRRRLLLLLLAALLLLAL-----------------AAAAAAAQAGPLLWKVSKGG--KTSYLFGTIHVLDPRDYPLPPAV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289   81 YKAIKSVDVVALEQNPEVWQEAYSREDFNGGNDFIHSQLfrsfnmsNERLTEQTF-SLSNYESKIQLGLASEARM----V 155
Cdd:COG3735     62 EEALAAADTLVLELDPDDPDALALQALMKLMLLPDGKTL-------SDLLSPEEYaRLEALLAALGLPLAALARLkpwfA 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  156 NGMLYRNNVGQEDFEEETYLDMYIYRLGRKLNKIVTGVEDYKES----DKLVKEAYRDMYKD-----KKPRRSYDisgfd 226
Cdd:COG3735    135 ALLLSLAALQKAGLDPETGVDMYLLKLAKAAGKPVVGLETVEEQlallDSLPEEEQAEMLREtldelEKGEAQLE----- 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  227 ykhKMEDAYRKG-DLDLLDSLQDITTVSDAFNEKFLFRRNDIQANSIDTILKKH-SLFVGVGAAHLPGERGVIELLRKKG 304
Cdd:COG3735    210 ---TLVDAWRAGdLAALEALLREDMAAYPEFYEALLDDRNRNWAPRIEALLKEPgTVFVAVGALHLPGEDGVLALLRARG 286

                   ....*.
gi 1721658289  305 YTVRPV 310
Cdd:COG3735    287 YTVERV 292
Tiki cd14789
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
48-307 1.42e-36

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: 139.36  E-value: 1.42e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289   48 LWEITGNGLvkPSYLFGTMHISNKMVFNLSDSFYKAIKSVDVVALE---QNPEVWQEAYSREDFNGGNDFIhsqlfrsfn 124
Cdd:cd14789      1 LWKISKGGL--TSYLFGTIHVGDPDVYPLPPAVEQALAASDALVLEldlTDPAALAALQAAMALPPDGKTL--------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  125 msNERLTEQTFS-LSNYESKIQLGLASEARM----VNGMLYRNNVGQEDFEEETYLDMYIYRLGRKLNKIVTGVEDYKES 199
Cdd:cd14789     70 --KDLLSPEDYArLKAALAELGLPLAALDKLkpwlLALTLSQLQLQKLGYDPEYGVDLYLAQRAKAAGKPVLGLETVEEQ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  200 ----DKLVKEAYRDMYKDKKPRRSYDISGFDykhKMEDAYRKG--DLDLLDSLQDITTVSDAFNEKFLFRRNDIQANSID 273
Cdd:cd14789    148 ldllDSLPEEEQLALLRSTLDELEEAEAELE---TLIEAWKAGdlDALEELLDESMKEDDPELYERLLVDRNRNWAPKIE 224
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1721658289  274 TIL-KKHSLFVGVGAAHLPGERGVIELLRKKGYTV 307
Cdd:cd14789    225 ALLkKGGTVFVAVGAGHLVGEDGLLALLRKKGYTV 259
TraB_PrgY_gumN pfam01963
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
47-309 2.35e-34

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: 132.86  E-value: 2.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289   47 LLWEITGNGLvkPSYLFGTMHISNKMVFNLSDSFYKAIKSVDVVALEQNPEvwqeaySREDFNGGNDFIHSQLFRSFNMS 126
Cdd:pfam01963    1 ALWKISKGGT--TVYLLGTIHVLPPSVYPLPPAIEEALEAADTVVVELDLS------RYTDPATQAALPKLGLLPDGKTL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  127 NERLTEQTF-SLSNYESKIQLGLASEARMVNGMLYRNNVGQEDFEE-----ETYLDMYIYRLGRKLNKIVTGVEDYKE-- 198
Cdd:pfam01963   73 SDLLSPELYaRLQKALAKRGLPLAALDRMKPWLAALLLSLAELAKQkagldPDLVDRYLAKTAKRAGKPVGGLETVEEql 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  199 -----SDKLVKEAYRDMYKD-KKPRRSYDisgfdykhKMEDAYRKGDLDLLDSLQDITTVSDAFNEKFLFRRNDIQANSI 272
Cdd:pfam01963  153 allslPDEEQLEMLEETLDElEKGEDLLE--------TLVEAWAEGDLEALELEAELKEAYPELYEVLLDERNRYWAEKI 224
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1721658289  273 DTILKK-HSLFVGVGAAHLPGERGVIELLRKKGYTVRP 309
Cdd:pfam01963  225 EALLKEgGTVFVAVGAGHLPGEDGVLALLRKKGYTVER 262
 
Name Accession Description Interval E-value
TraB COG3735
Uncharacterized conserved protein YbaP, TraB family [Function unknown];
1-310 6.92e-53

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


Pssm-ID: 442949  Cd Length: 293  Bit Score: 187.48  E-value: 6.92e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289    1 MKMKIVFVLLSISVVLFAnpfksfsqkkntdsksnTAAANQKKYPSLLWEITGNGlvKPSYLFGTMHISNKMVFNLSDSF 80
Cdd:COG3735      1 MRRRLLLLLLAALLLLAL-----------------AAAAAAAQAGPLLWKVSKGG--KTSYLFGTIHVLDPRDYPLPPAV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289   81 YKAIKSVDVVALEQNPEVWQEAYSREDFNGGNDFIHSQLfrsfnmsNERLTEQTF-SLSNYESKIQLGLASEARM----V 155
Cdd:COG3735     62 EEALAAADTLVLELDPDDPDALALQALMKLMLLPDGKTL-------SDLLSPEEYaRLEALLAALGLPLAALARLkpwfA 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  156 NGMLYRNNVGQEDFEEETYLDMYIYRLGRKLNKIVTGVEDYKES----DKLVKEAYRDMYKD-----KKPRRSYDisgfd 226
Cdd:COG3735    135 ALLLSLAALQKAGLDPETGVDMYLLKLAKAAGKPVVGLETVEEQlallDSLPEEEQAEMLREtldelEKGEAQLE----- 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  227 ykhKMEDAYRKG-DLDLLDSLQDITTVSDAFNEKFLFRRNDIQANSIDTILKKH-SLFVGVGAAHLPGERGVIELLRKKG 304
Cdd:COG3735    210 ---TLVDAWRAGdLAALEALLREDMAAYPEFYEALLDDRNRNWAPRIEALLKEPgTVFVAVGALHLPGEDGVLALLRARG 286

                   ....*.
gi 1721658289  305 YTVRPV 310
Cdd:COG3735    287 YTVERV 292
Tiki cd14789
Tiki homology domain antagonizes Wnt function via cleavage of amino-terminal residues; Tiki is ...
48-307 1.42e-36

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: 139.36  E-value: 1.42e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289   48 LWEITGNGLvkPSYLFGTMHISNKMVFNLSDSFYKAIKSVDVVALE---QNPEVWQEAYSREDFNGGNDFIhsqlfrsfn 124
Cdd:cd14789      1 LWKISKGGL--TSYLFGTIHVGDPDVYPLPPAVEQALAASDALVLEldlTDPAALAALQAAMALPPDGKTL--------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  125 msNERLTEQTFS-LSNYESKIQLGLASEARM----VNGMLYRNNVGQEDFEEETYLDMYIYRLGRKLNKIVTGVEDYKES 199
Cdd:cd14789     70 --KDLLSPEDYArLKAALAELGLPLAALDKLkpwlLALTLSQLQLQKLGYDPEYGVDLYLAQRAKAAGKPVLGLETVEEQ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  200 ----DKLVKEAYRDMYKDKKPRRSYDISGFDykhKMEDAYRKG--DLDLLDSLQDITTVSDAFNEKFLFRRNDIQANSID 273
Cdd:cd14789    148 ldllDSLPEEEQLALLRSTLDELEEAEAELE---TLIEAWKAGdlDALEELLDESMKEDDPELYERLLVDRNRNWAPKIE 224
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1721658289  274 TIL-KKHSLFVGVGAAHLPGERGVIELLRKKGYTV 307
Cdd:cd14789    225 ALLkKGGTVFVAVGAGHLVGEDGLLALLRKKGYTV 259
TraB_PrgY_gumN pfam01963
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
47-309 2.35e-34

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: 132.86  E-value: 2.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289   47 LLWEITGNGLvkPSYLFGTMHISNKMVFNLSDSFYKAIKSVDVVALEQNPEvwqeaySREDFNGGNDFIHSQLFRSFNMS 126
Cdd:pfam01963    1 ALWKISKGGT--TVYLLGTIHVLPPSVYPLPPAIEEALEAADTVVVELDLS------RYTDPATQAALPKLGLLPDGKTL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  127 NERLTEQTF-SLSNYESKIQLGLASEARMVNGMLYRNNVGQEDFEE-----ETYLDMYIYRLGRKLNKIVTGVEDYKE-- 198
Cdd:pfam01963   73 SDLLSPELYaRLQKALAKRGLPLAALDRMKPWLAALLLSLAELAKQkagldPDLVDRYLAKTAKRAGKPVGGLETVEEql 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721658289  199 -----SDKLVKEAYRDMYKD-KKPRRSYDisgfdykhKMEDAYRKGDLDLLDSLQDITTVSDAFNEKFLFRRNDIQANSI 272
Cdd:pfam01963  153 allslPDEEQLEMLEETLDElEKGEDLLE--------TLVEAWAEGDLEALELEAELKEAYPELYEVLLDERNRYWAEKI 224
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1721658289  273 DTILKK-HSLFVGVGAAHLPGERGVIELLRKKGYTVRP 309
Cdd:pfam01963  225 EALLKEgGTVFVAVGAGHLPGEDGVLALLRKKGYTVER 262
 
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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