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Conserved domains on  [gi|981394976|ref|WP_059607713|]
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DUF3857 domain-containing transglutaminase family protein [Burkholderia vietnamiensis]

Protein Classification

DUF3857 domain-containing transglutaminase family protein( domain architecture ID 12125919)

DUF3857 domain-containing transglutaminase family protein may act as a cysteine protease

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3857 pfam12969
Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first ...
 58-188 1.47e-22

Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first domain of the PDB structure PDB:3KD4(residues 1-228). It is structurally similar to domains in other hydrolases, eg. M1 family aminopeptidase (3ebi, Z=10, rmsd 3.6A for 152 CA, seq id 12%), despite lack of any significant sequence similarity.


:

Pssm-ID: 432907 [Multi-domain]  Cd Length: 131  Bit Score: 93.52  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976   58 DGSLDEDDDSTLRANDASGIDAIAQRYVWYDKNLEKVELVAAETIDRDSVAHPVGADGIRDVQEPRSAGAPTFQDGLLRT 137
Cdd:pfam12969   1 DGSGERTVHKVVTILTEAGVESYSEIFISYDPDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAADAPLYSDARVKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 981394976  138 VVFPGVEAGSRTRIAFRKSRTKPVNAGYFGYYVEPSREPVEHQRLIFDVPA 188
Cdd:pfam12969  81 IVLPDVRVGDTVEYEYTITGKNPVFGGFSDSEPFQQFSPVLRSRLRVIVPA 131
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 209-378 2.50e-16

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 76.97  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976 209 GRTRYAFDYRHGPYERIESGSVGYQTYGDRLVVSTLPDYAAFAARYRNAAVDAGAHDPAVVQLARALTADADGARDKARI 288
Cdd:COG1305    4 LVLAALLAALSGPLAPAPTGLLVTAGAGRGGGVASVVPGGGTELLAGPGELLSASYDPELRALAAELTGGATTPYEKARA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976 289 LYDWVQANVRYVAiflgETAAAPHRVTDILRNRYGDCKDHVALFGALLAAVGIRSEPVlisLGAVYTLPSvPGYGGGAIN 368
Cdd:COG1305   84 LYDWVRDNIRYDP----GSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYV---SGYLPGEPP-PGGGRADDA 155

                        170
                 ....*....|..
gi 981394976 369 HAIT--WLPELG 378
Cdd:COG1305  156 HAWVevYLPGAG 167
 
Name Accession Description Interval E-value
DUF3857 pfam12969
Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first ...
 58-188 1.47e-22

Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first domain of the PDB structure PDB:3KD4(residues 1-228). It is structurally similar to domains in other hydrolases, eg. M1 family aminopeptidase (3ebi, Z=10, rmsd 3.6A for 152 CA, seq id 12%), despite lack of any significant sequence similarity.


Pssm-ID: 432907 [Multi-domain]  Cd Length: 131  Bit Score: 93.52  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976   58 DGSLDEDDDSTLRANDASGIDAIAQRYVWYDKNLEKVELVAAETIDRDSVAHPVGADGIRDVQEPRSAGAPTFQDGLLRT 137
Cdd:pfam12969   1 DGSGERTVHKVVTILTEAGVESYSEIFISYDPDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAADAPLYSDARVKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 981394976  138 VVFPGVEAGSRTRIAFRKSRTKPVNAGYFGYYVEPSREPVEHQRLIFDVPA 188
Cdd:pfam12969  81 IVLPDVRVGDTVEYEYTITGKNPVFGGFSDSEPFQQFSPVLRSRLRVIVPA 131
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 209-378 2.50e-16

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 76.97  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976 209 GRTRYAFDYRHGPYERIESGSVGYQTYGDRLVVSTLPDYAAFAARYRNAAVDAGAHDPAVVQLARALTADADGARDKARI 288
Cdd:COG1305    4 LVLAALLAALSGPLAPAPTGLLVTAGAGRGGGVASVVPGGGTELLAGPGELLSASYDPELRALAAELTGGATTPYEKARA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976 289 LYDWVQANVRYVAiflgETAAAPHRVTDILRNRYGDCKDHVALFGALLAAVGIRSEPVlisLGAVYTLPSvPGYGGGAIN 368
Cdd:COG1305   84 LYDWVRDNIRYDP----GSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYV---SGYLPGEPP-PGGGRADDA 155

                        170
                 ....*....|..
gi 981394976 369 HAIT--WLPELG 378
Cdd:COG1305  156 HAWVevYLPGAG 167
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 270-341 1.19e-09

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 55.87  E-value: 1.19e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981394976  270 QLARALTADADGARDKARILYDWVQANVRYVaifLGETAAAPHRVTDILRNRYGDCKDHVALFGALLAAVGI 341
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYD---LPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGI 70
 
Name Accession Description Interval E-value
DUF3857 pfam12969
Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first ...
 58-188 1.47e-22

Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first domain of the PDB structure PDB:3KD4(residues 1-228). It is structurally similar to domains in other hydrolases, eg. M1 family aminopeptidase (3ebi, Z=10, rmsd 3.6A for 152 CA, seq id 12%), despite lack of any significant sequence similarity.


Pssm-ID: 432907 [Multi-domain]  Cd Length: 131  Bit Score: 93.52  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976   58 DGSLDEDDDSTLRANDASGIDAIAQRYVWYDKNLEKVELVAAETIDRDSVAHPVGADGIRDVQEPRSAGAPTFQDGLLRT 137
Cdd:pfam12969   1 DGSGERTVHKVVTILTEAGVESYSEIFISYDPDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAADAPLYSDARVKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 981394976  138 VVFPGVEAGSRTRIAFRKSRTKPVNAGYFGYYVEPSREPVEHQRLIFDVPA 188
Cdd:pfam12969  81 IVLPDVRVGDTVEYEYTITGKNPVFGGFSDSEPFQQFSPVLRSRLRVIVPA 131
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 209-378 2.50e-16

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 76.97  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976 209 GRTRYAFDYRHGPYERIESGSVGYQTYGDRLVVSTLPDYAAFAARYRNAAVDAGAHDPAVVQLARALTADADGARDKARI 288
Cdd:COG1305    4 LVLAALLAALSGPLAPAPTGLLVTAGAGRGGGVASVVPGGGTELLAGPGELLSASYDPELRALAAELTGGATTPYEKARA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981394976 289 LYDWVQANVRYVAiflgETAAAPHRVTDILRNRYGDCKDHVALFGALLAAVGIRSEPVlisLGAVYTLPSvPGYGGGAIN 368
Cdd:COG1305   84 LYDWVRDNIRYDP----GSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYV---SGYLPGEPP-PGGGRADDA 155

                        170
                 ....*....|..
gi 981394976 369 HAIT--WLPELG 378
Cdd:COG1305  156 HAWVevYLPGAG 167
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 270-341 1.19e-09

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 55.87  E-value: 1.19e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981394976  270 QLARALTADADGARDKARILYDWVQANVRYVaifLGETAAAPHRVTDILRNRYGDCKDHVALFGALLAAVGI 341
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYD---LPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGI 70
 
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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