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Conserved domains on  [gi|491939881|ref|WP_005682577|]
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MULTISPECIES: DUF3857 domain-containing protein [Bacteroides]

Protein Classification

DUF3857 and YebA domain-containing protein( domain architecture ID 12125926)

protein containing domains DUF3857, YebA, and DUF3858

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 ...
 56-197 5.20e-34

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: 126.27  E-value: 5.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881   56 GQGSFAVCKVIKVQTPRGAVANRVIKYDYDPLTAYAEFKRVTVYRANGKVDELDVKKTCDYAAPARA---IYWGARQIML 132
Cdd:pfam12969   2 GSGERTVHKVVTILTEAGVESYSEIFISYDPDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAAdapLYSDARVKVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491939881  133 EIGALQPGDVVDYEIAKKGFTyallgagdeddsrfipPMRGQFYDIVPFWSAAPTVRKVYKVAVP 197
Cdd:pfam12969  82 VLPDVRVGDTVEYEYTITGKN----------------PVFGGFSDSEPFQQFSPVLRSRLRVIVP 130
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 224-396 8.48e-15

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


:

Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 72.73  E-value: 8.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881 224 YTFAMDNVMPFGREPNMVDLFDAAPKLMMSSTPQWKDKSLWFNKVNEDYGSFAPL-PEAQKKVDELIKGKKTEMEKIAVL 302
Cdd:COG1305    5 VLAALLAALSGPLAPAPTGLLVTAGAGRGGGVASVVPGGGTELLAGPGELLSASYdPELRALAAELTGGATTPYEKARAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881 303 THWVADNIRYaGISMGkGEGFTLHNTkmnYTDRCGVCKDIAGTLISFLRMAGFEAYPAM-TMAGSRVESIPADHFNHCVA 381
Cdd:COG1305   85 YDWVRDNIRY-DPGST-GVGTTALET---LERRRGVCRDFAHLLVALLRALGIPARYVSgYLPGEPPPGGGRADDAHAWV 159

                        170
                 ....*....|....*
gi 491939881 382 VVKLSNGTYMPLDPT 396
Cdd:COG1305  160 EVYLPGAGWVPFDPT 174
DUF3858 super family cl15204
Domain of Unknown Function with PDB structure (DUF3858); This family is based on the third ...
 576-634 1.33e-03

Domain of Unknown Function with PDB structure (DUF3858); This family is based on the third domain of the PDB structure 3KD4(residues 410-525). It is structurally similar to part of neuropilin-2 (Z=4.6, rmsd 3.6A for 83 CA, 7% seq id). This domain and the second domain appears to be part of peptide-n-glycanase (1x3w, 2g9f).


The actual alignment was detected with superfamily member pfam12970:

Pssm-ID: 404007  Cd Length: 116  Bit Score: 38.88  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491939881  576 TIQLPAGYKLANADKNETMQGTGADFEGSLAQQGNKVLLHNKLALKKRVYEAADWDSFR 634
Cdd:pfam12970  42 TVKVPDGLKLVTKPQEKKISNPVGSVSITIKQEGNKVEIIRTLKLNKQLITPAEYPAFR 100
 
Name Accession Description Interval E-value
DUF3857 pfam12969
Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first ...
 56-197 5.20e-34

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: 126.27  E-value: 5.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881   56 GQGSFAVCKVIKVQTPRGAVANRVIKYDYDPLTAYAEFKRVTVYRANGKVDELDVKKTCDYAAPARA---IYWGARQIML 132
Cdd:pfam12969   2 GSGERTVHKVVTILTEAGVESYSEIFISYDPDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAAdapLYSDARVKVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491939881  133 EIGALQPGDVVDYEIAKKGFTyallgagdeddsrfipPMRGQFYDIVPFWSAAPTVRKVYKVAVP 197
Cdd:pfam12969  82 VLPDVRVGDTVEYEYTITGKN----------------PVFGGFSDSEPFQQFSPVLRSRLRVIVP 130
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 224-396 8.48e-15

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 72.73  E-value: 8.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881 224 YTFAMDNVMPFGREPNMVDLFDAAPKLMMSSTPQWKDKSLWFNKVNEDYGSFAPL-PEAQKKVDELIKGKKTEMEKIAVL 302
Cdd:COG1305    5 VLAALLAALSGPLAPAPTGLLVTAGAGRGGGVASVVPGGGTELLAGPGELLSASYdPELRALAAELTGGATTPYEKARAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881 303 THWVADNIRYaGISMGkGEGFTLHNTkmnYTDRCGVCKDIAGTLISFLRMAGFEAYPAM-TMAGSRVESIPADHFNHCVA 381
Cdd:COG1305   85 YDWVRDNIRY-DPGST-GVGTTALET---LERRRGVCRDFAHLLVALLRALGIPARYVSgYLPGEPPPGGGRADDAHAWV 159

                        170
                 ....*....|....*
gi 491939881 382 VVKLSNGTYMPLDPT 396
Cdd:COG1305  160 EVYLPGAGWVPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 285-395 4.76e-08

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: 51.64  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881  285 VDELIKGKKTEMEKIAVLTHWVADNIRYAGI----SMGKGEGFtlhntkmnYTDRCGVCKDIAGTLISFLRMAGFeayPA 360
Cdd:pfam01841   4 ADRITGGATDPLEKARAIYDYVRKNITYDLPgrspGDGDAEEF--------LFTGKGDCEDFASLFVALLRALGI---PA 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 491939881  361 MTMAGSRVESIPADHFN-HCVAVVKLSNGTYMPLDP 395
Cdd:pfam01841  73 RYVTGYLRGPDTVRGGDaHAWVEVYLPGYGWVPVDP 108
DUF3858 pfam12970
Domain of Unknown Function with PDB structure (DUF3858); This family is based on the third ...
 576-634 1.33e-03

Domain of Unknown Function with PDB structure (DUF3858); This family is based on the third domain of the PDB structure 3KD4(residues 410-525). It is structurally similar to part of neuropilin-2 (Z=4.6, rmsd 3.6A for 83 CA, 7% seq id). This domain and the second domain appears to be part of peptide-n-glycanase (1x3w, 2g9f).


Pssm-ID: 404007  Cd Length: 116  Bit Score: 38.88  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491939881  576 TIQLPAGYKLANADKNETMQGTGADFEGSLAQQGNKVLLHNKLALKKRVYEAADWDSFR 634
Cdd:pfam12970  42 TVKVPDGLKLVTKPQEKKISNPVGSVSITIKQEGNKVEIIRTLKLNKQLITPAEYPAFR 100
 
Name Accession Description Interval E-value
DUF3857 pfam12969
Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first ...
 56-197 5.20e-34

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: 126.27  E-value: 5.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881   56 GQGSFAVCKVIKVQTPRGAVANRVIKYDYDPLTAYAEFKRVTVYRANGKVDELDVKKTCDYAAPARA---IYWGARQIML 132
Cdd:pfam12969   2 GSGERTVHKVVTILTEAGVESYSEIFISYDPDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAAdapLYSDARVKVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491939881  133 EIGALQPGDVVDYEIAKKGFTyallgagdeddsrfipPMRGQFYDIVPFWSAAPTVRKVYKVAVP 197
Cdd:pfam12969  82 VLPDVRVGDTVEYEYTITGKN----------------PVFGGFSDSEPFQQFSPVLRSRLRVIVP 130
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 224-396 8.48e-15

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 72.73  E-value: 8.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881 224 YTFAMDNVMPFGREPNMVDLFDAAPKLMMSSTPQWKDKSLWFNKVNEDYGSFAPL-PEAQKKVDELIKGKKTEMEKIAVL 302
Cdd:COG1305    5 VLAALLAALSGPLAPAPTGLLVTAGAGRGGGVASVVPGGGTELLAGPGELLSASYdPELRALAAELTGGATTPYEKARAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881 303 THWVADNIRYaGISMGkGEGFTLHNTkmnYTDRCGVCKDIAGTLISFLRMAGFEAYPAM-TMAGSRVESIPADHFNHCVA 381
Cdd:COG1305   85 YDWVRDNIRY-DPGST-GVGTTALET---LERRRGVCRDFAHLLVALLRALGIPARYVSgYLPGEPPPGGGRADDAHAWV 159

                        170
                 ....*....|....*
gi 491939881 382 VVKLSNGTYMPLDPT 396
Cdd:COG1305  160 EVYLPGAGWVPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 285-395 4.76e-08

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: 51.64  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491939881  285 VDELIKGKKTEMEKIAVLTHWVADNIRYAGI----SMGKGEGFtlhntkmnYTDRCGVCKDIAGTLISFLRMAGFeayPA 360
Cdd:pfam01841   4 ADRITGGATDPLEKARAIYDYVRKNITYDLPgrspGDGDAEEF--------LFTGKGDCEDFASLFVALLRALGI---PA 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 491939881  361 MTMAGSRVESIPADHFN-HCVAVVKLSNGTYMPLDP 395
Cdd:pfam01841  73 RYVTGYLRGPDTVRGGDaHAWVEVYLPGYGWVPVDP 108
DUF3858 pfam12970
Domain of Unknown Function with PDB structure (DUF3858); This family is based on the third ...
 576-634 1.33e-03

Domain of Unknown Function with PDB structure (DUF3858); This family is based on the third domain of the PDB structure 3KD4(residues 410-525). It is structurally similar to part of neuropilin-2 (Z=4.6, rmsd 3.6A for 83 CA, 7% seq id). This domain and the second domain appears to be part of peptide-n-glycanase (1x3w, 2g9f).


Pssm-ID: 404007  Cd Length: 116  Bit Score: 38.88  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491939881  576 TIQLPAGYKLANADKNETMQGTGADFEGSLAQQGNKVLLHNKLALKKRVYEAADWDSFR 634
Cdd:pfam12970  42 TVKVPDGLKLVTKPQEKKISNPVGSVSITIKQEGNKVEIIRTLKLNKQLITPAEYPAFR 100
 
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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