NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2167539922|ref|WP_232211404|]
View 

transglutaminase family protein [Odoribacter laneus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
133-228 2.10e-15

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


:

Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 73.50  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2167539922 133 SYVANCQTIWEAIDSVNRNIRDEVRvdYNTKREKPDQSPYESMRQGMASCSGLSILLTDAFRAVGIPARVA-------GT 205
Cdd:COG1305    69 ELTGGATTPYEKARALYDWVRDNIR--YDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVsgylpgePP 146
                          90       100
                  ....*....|....*....|....
gi 2167539922 206 PNWHDNRGNHNWCEVWVDGQ-WYF 228
Cdd:COG1305   147 PGGGRADDAHAWVEVYLPGAgWVP 170
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
133-228 2.10e-15

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 73.50  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2167539922 133 SYVANCQTIWEAIDSVNRNIRDEVRvdYNTKREKPDQSPYESMRQGMASCSGLSILLTDAFRAVGIPARVA-------GT 205
Cdd:COG1305    69 ELTGGATTPYEKARALYDWVRDNIR--YDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVsgylpgePP 146
                          90       100
                  ....*....|....*....|....
gi 2167539922 206 PNWHDNRGNHNWCEVWVDGQ-WYF 228
Cdd:COG1305   147 PGGGRADDAHAWVEVYLPGAgWVP 170
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
135-227 5.61e-10

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: 56.26  E-value: 5.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2167539922 135 VANCQTIWEAIDSVNRNIRDEVRVDYNTkREKPDQSPYESMRQGMASCSGLSILLTDAFRAVGIPARVAGTPNWH----D 210
Cdd:pfam01841   8 TGGATDPLEKARAIYDYVRKNITYDLPG-RSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRGpdtvR 86
                          90
                  ....*....|....*...
gi 2167539922 211 NRGNHNWCEVWVDGQ-WY 227
Cdd:pfam01841  87 GGDAHAWVEVYLPGYgWV 104
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
175-228 7.88e-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: 48.92  E-value: 7.88e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2167539922  175 MRQGMASCSGLSILLTDAFRAVGIPARVAG--------TPNWHDNRGNHNWCEVWVDGQWYF 228
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSgylkapdtIGGLRSIWEAHAWAEVYLEGGWVP 63
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
133-228 2.10e-15

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 73.50  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2167539922 133 SYVANCQTIWEAIDSVNRNIRDEVRvdYNTKREKPDQSPYESMRQGMASCSGLSILLTDAFRAVGIPARVA-------GT 205
Cdd:COG1305    69 ELTGGATTPYEKARALYDWVRDNIR--YDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVsgylpgePP 146
                          90       100
                  ....*....|....*....|....
gi 2167539922 206 PNWHDNRGNHNWCEVWVDGQ-WYF 228
Cdd:COG1305   147 PGGGRADDAHAWVEVYLPGAgWVP 170
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
135-227 5.61e-10

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: 56.26  E-value: 5.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2167539922 135 VANCQTIWEAIDSVNRNIRDEVRVDYNTkREKPDQSPYESMRQGMASCSGLSILLTDAFRAVGIPARVAGTPNWH----D 210
Cdd:pfam01841   8 TGGATDPLEKARAIYDYVRKNITYDLPG-RSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRGpdtvR 86
                          90
                  ....*....|....*...
gi 2167539922 211 NRGNHNWCEVWVDGQ-WY 227
Cdd:pfam01841  87 GGDAHAWVEVYLPGYgWV 104
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
175-228 7.88e-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: 48.92  E-value: 7.88e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2167539922  175 MRQGMASCSGLSILLTDAFRAVGIPARVAG--------TPNWHDNRGNHNWCEVWVDGQWYF 228
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSgylkapdtIGGLRSIWEAHAWAEVYLEGGWVP 63
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
159-227 3.45e-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: 3.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2167539922 159 DYNTKREKP--DQSPYESMRQGMASCSGLSILLTDAFRAVGIPAR-VAGTPNWHDNR-GNHNWCEVWVDGQWY 227
Cdd:COG5279   119 DYEAYNSGKsdSHSAYGALKNGKGVCEGYAKLFKLLCNKAGIECYiVTGYARGSGGEsGNHAWNAVKIDGKWY 191
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH