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Conserved domains on  [gi|490726384|ref|WP_004588887|]
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MULTISPECIES: transglutaminase family protein [Gammaproteobacteria]

Protein Classification

transglutaminase-like domain-containing protein( domain architecture ID 11441893)

transglutaminase-like domain-containing protein may act as a cysteine protease

CATH:  3.10.620.30
PubMed:  10452618|15288868

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 19-134 1.28e-15

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


:

Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 72.34  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726384  19 IQSLISERNWQELDDFNKIGAAYQFVKDEILFGYNESD-DISASSVLADGYGQCNTKGNLLMALLRGLGIQCRFHGFTIE 97
Cdd:COG1305   63 LRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGvGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSGYLP 142

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490726384  98 QRLQKGAIPTYVFwlapkyiiHSWIEVYFKDR-WINLE 134
Cdd:COG1305  143 GEPPPGGGRADDA--------HAWVEVYLPGAgWVPFD 172
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 19-134 1.28e-15

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 72.34  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726384  19 IQSLISERNWQELDDFNKIGAAYQFVKDEILFGYNESD-DISASSVLADGYGQCNTKGNLLMALLRGLGIQCRFHGFTIE 97
Cdd:COG1305   63 LRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGvGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSGYLP 142

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490726384  98 QRLQKGAIPTYVFwlapkyiiHSWIEVYFKDR-WINLE 134
Cdd:COG1305  143 GEPPPGGGRADDA--------HAWVEVYLPGAgWVPFD 172
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 30-134 3.58e-11

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: 58.57  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726384   30 ELDDFNKIGAAYQFVKDEILFGYNESD--DISASSVLADGYGQCNTKGNLLMALLRGLGIQCRF-HGFTIEQrlqkgaip 106
Cdd:pfam01841  11 ATDPLEKARAIYDYVRKNITYDLPGRSpgDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYvTGYLRGP-------- 82

                          90       100
                  ....*....|....*....|....*....
gi 490726384  107 tyvfWLAPKYIIHSWIEVYFKD-RWINLE 134
Cdd:pfam01841  83 ----DTVRGGDAHAWVEVYLPGyGWVPVD 107
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 63-134 2.60e-08

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: 49.30  E-value: 2.60e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726384    63 VLADGYGQCNTKGNLLMALLRGLGIQCRF-HGFTIEQRLQKGaipTYVFWLApkyiiHSWIEVYFKDRWINLE 134
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVvSGYLKAPDTIGG---LRSIWEA-----HAWAEVYLEGGWVPVD 65
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 19-134 1.28e-15

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 72.34  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726384  19 IQSLISERNWQELDDFNKIGAAYQFVKDEILFGYNESD-DISASSVLADGYGQCNTKGNLLMALLRGLGIQCRFHGFTIE 97
Cdd:COG1305   63 LRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGvGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSGYLP 142

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490726384  98 QRLQKGAIPTYVFwlapkyiiHSWIEVYFKDR-WINLE 134
Cdd:COG1305  143 GEPPPGGGRADDA--------HAWVEVYLPGAgWVPFD 172
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 30-134 3.58e-11

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: 58.57  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726384   30 ELDDFNKIGAAYQFVKDEILFGYNESD--DISASSVLADGYGQCNTKGNLLMALLRGLGIQCRF-HGFTIEQrlqkgaip 106
Cdd:pfam01841  11 ATDPLEKARAIYDYVRKNITYDLPGRSpgDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYvTGYLRGP-------- 82

                          90       100
                  ....*....|....*....|....*....
gi 490726384  107 tyvfWLAPKYIIHSWIEVYFKD-RWINLE 134
Cdd:pfam01841  83 ----DTVRGGDAHAWVEVYLPGyGWVPVD 107
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 63-134 2.60e-08

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: 49.30  E-value: 2.60e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726384    63 VLADGYGQCNTKGNLLMALLRGLGIQCRF-HGFTIEQRLQKGaipTYVFWLApkyiiHSWIEVYFKDRWINLE 134
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVvSGYLKAPDTIGG---LRSIWEA-----HAWAEVYLEGGWVPVD 65
 
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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