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Conserved domains on  [gi|15597240|ref|NP_250734|]
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hypothetical protein PA2044 [Pseudomonas aeruginosa PAO1]

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 ...
 47-174 3.27e-15

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: 72.72  E-value: 3.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240    47 DNSTDCVSTYSFTILKPSGREMLSRIDRSYA-ETDSLIVEKAELTQPGGKPVPLDQSQIDTRTAPNPDQGFLRE--RQTS 123
Cdd:pfam12969   1 DGSGERTVHKVVTILTEAGVESYSEIFISYDpDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAADAPLYSdaRVKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597240   124 LAFPNLRVGTRISYTLREHFTaKPLSTQFHYILSRP-PMPVRDDRFVAEFKA 174
Cdd:pfam12969  81 IVLPDVRVGDTVEYEYTITGK-NPVFGGFSDSEPFQqFSPVLRSRLRVIVPA 131
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 268-372 1.67e-13

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


:

Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 68.88  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240 268 PAREQVAGLMQYINDTYRYlgdwrASERGYVPFSLAEIERNGYGDCKDLAILLAAMLKAAGIKAEptLVSRgdVVWDLLV 347
Cdd:COG1305  76 TPYEKARALYDWVRDNIRY-----DPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPAR--YVSG--YLPGEPP 146

                        90       100
                ....*....|....*....|....*...
gi 15597240 348 PGMYAP--NHAIVRAEVDGKTW-WLDPT 372
Cdd:COG1305 147 PGGGRAddAHAWVEVYLPGAGWvPFDPT 174
 
Name Accession Description Interval E-value
DUF3857 pfam12969
Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first ...
 47-174 3.27e-15

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: 72.72  E-value: 3.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240    47 DNSTDCVSTYSFTILKPSGREMLSRIDRSYA-ETDSLIVEKAELTQPGGKPVPLDQSQIDTRTAPNPDQGFLRE--RQTS 123
Cdd:pfam12969   1 DGSGERTVHKVVTILTEAGVESYSEIFISYDpDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAADAPLYSdaRVKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597240   124 LAFPNLRVGTRISYTLREHFTaKPLSTQFHYILSRP-PMPVRDDRFVAEFKA 174
Cdd:pfam12969  81 IVLPDVRVGDTVEYEYTITGK-NPVFGGFSDSEPFQqFSPVLRSRLRVIVPA 131
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 268-372 1.67e-13

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 68.88  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240 268 PAREQVAGLMQYINDTYRYlgdwrASERGYVPFSLAEIERNGYGDCKDLAILLAAMLKAAGIKAEptLVSRgdVVWDLLV 347
Cdd:COG1305  76 TPYEKARALYDWVRDNIRY-----DPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPAR--YVSG--YLPGEPP 146

                        90       100
                ....*....|....*....|....*...
gi 15597240 348 PGMYAP--NHAIVRAEVDGKTW-WLDPT 372
Cdd:COG1305 147 PGGGRAddAHAWVEVYLPGAGWvPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 268-371 1.92e-06

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: 46.63  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240   268 PAREQVAGLMQYINDTYRYlgdwRASERGYVPFSLAEIERNGYGDCKDLAILLAAMLKAAGIkaePTLVSRGDVVWDLLV 347
Cdd:pfam01841  13 DPLEKARAIYDYVRKNITY----DLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGI---PARYVTGYLRGPDTV 85

                          90       100
                  ....*....|....*....|....*
gi 15597240   348 PGMYApnHAIVRAEVDGKTWW-LDP 371
Cdd:pfam01841  86 RGGDA--HAWVEVYLPGYGWVpVDP 108
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 305-373 7.96e-05

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 41.21  E-value: 7.96e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597240    305 IERNGYGDCKDLAILLAAMLKAAGIKAEptlvsrgdVVWDLLVPGMYAP-------NHAIVRAEVDGKtWW-LDPTN 373
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPAR--------VVSGYLKAPDTIGglrsiweAHAWAEVYLEGG-WVpVDPTP 68
 
Name Accession Description Interval E-value
DUF3857 pfam12969
Domain of Unknown Function with PDB structure (DUF3857); This family is based on the first ...
 47-174 3.27e-15

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: 72.72  E-value: 3.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240    47 DNSTDCVSTYSFTILKPSGREMLSRIDRSYA-ETDSLIVEKAELTQPGGKPVPLDQSQIDTRTAPNPDQGFLRE--RQTS 123
Cdd:pfam12969   1 DGSGERTVHKVVTILTEAGVESYSEIFISYDpDFQKLKIHRARVIRPDGKVIKLDPSAIDEVDPPAAADAPLYSdaRVKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597240   124 LAFPNLRVGTRISYTLREHFTaKPLSTQFHYILSRP-PMPVRDDRFVAEFKA 174
Cdd:pfam12969  81 IVLPDVRVGDTVEYEYTITGK-NPVFGGFSDSEPFQqFSPVLRSRLRVIVPA 131
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 268-372 1.67e-13

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 68.88  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240 268 PAREQVAGLMQYINDTYRYlgdwrASERGYVPFSLAEIERNGYGDCKDLAILLAAMLKAAGIKAEptLVSRgdVVWDLLV 347
Cdd:COG1305  76 TPYEKARALYDWVRDNIRY-----DPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPAR--YVSG--YLPGEPP 146

                        90       100
                ....*....|....*....|....*...
gi 15597240 348 PGMYAP--NHAIVRAEVDGKTW-WLDPT 372
Cdd:COG1305 147 PGGGRAddAHAWVEVYLPGAGWvPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 268-371 1.92e-06

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: 46.63  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240   268 PAREQVAGLMQYINDTYRYlgdwRASERGYVPFSLAEIERNGYGDCKDLAILLAAMLKAAGIkaePTLVSRGDVVWDLLV 347
Cdd:pfam01841  13 DPLEKARAIYDYVRKNITY----DLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGI---PARYVTGYLRGPDTV 85

                          90       100
                  ....*....|....*....|....*
gi 15597240   348 PGMYApnHAIVRAEVDGKTWW-LDP 371
Cdd:pfam01841  86 RGGDA--HAWVEVYLPGYGWVpVDP 108
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 305-373 7.96e-05

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 41.21  E-value: 7.96e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597240    305 IERNGYGDCKDLAILLAAMLKAAGIKAEptlvsrgdVVWDLLVPGMYAP-------NHAIVRAEVDGKtWW-LDPTN 373
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPAR--------VVSGYLKAPDTIGglrsiweAHAWAEVYLEGG-WVpVDPTP 68
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 279-372 6.02e-04

Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444090 [Multi-domain]  Cd Length: 250  Bit Score: 41.92  E-value: 6.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597240 279 YINDTYRYlgDWRASERG-YVPFSLAEIERNGYGDCKDLAILLAAMLKAAGIKAEptlVSRGDVVwdllVPGMYAPNHA- 356
Cdd:COG5279 111 WIVDNIEY--DYEAYNSGkSDSHSAYGALKNGKGVCEGYAKLFKLLCNKAGIECY---IVTGYAR----GSGGESGNHAw 181

                        90
                ....*....|....*..
gi 15597240 357 -IVRaeVDGKTWWLDPT 372
Cdd:COG5279 182 nAVK--IDGKWYLVDAT 196
 
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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