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Conserved domains on  [gi|502304110|ref|WP_012757514|]
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transglutaminase family protein [Rhizobium leguminosarum]

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, ...
 113-226 3.04e-38

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


:

Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 132.44  E-value: 3.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304110 113 TDRLADFAWARFSSTPLGWARVQAICDFVHDHITFDYLKADVLRTAHGGFTDKAGVCRDFAHLAIALCRCMNIPARYCTG 192
Cdd:COG1305   60 DPELRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSG 139

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502304110 193 YLGDIGVPIDPNPMDFSAWFEVFLGGH-WHTVDAR 226
Cdd:COG1305  140 YLPGEPPPGGGRADDAHAWVEVYLPGAgWVPFDPT 174
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 113-226 3.04e-38

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 132.44  E-value: 3.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304110 113 TDRLADFAWARFSSTPLGWARVQAICDFVHDHITFDYLKADVLRTAHGGFTDKAGVCRDFAHLAIALCRCMNIPARYCTG 192
Cdd:COG1305   60 DPELRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSG 139

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502304110 193 YLGDIGVPIDPNPMDFSAWFEVFLGGH-WHTVDAR 226
Cdd:COG1305  140 YLPGEPPPGGGRADDAHAWVEVYLPGAgWVPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 133-225 3.03e-17

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: 75.13  E-value: 3.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304110  133 RVQAICDFVHDHITFDYLKA-----DVLRTahggFTDKAGVCRDFAHLAIALCRCMNIPARYCTGYLGDigvPIDPNPMD 207
Cdd:pfam01841  17 KARAIYDYVRKNITYDLPGRspgdgDAEEF----LFTGKGDCEDFASLFVALLRALGIPARYVTGYLRG---PDTVRGGD 89

                          90
                  ....*....|....*....
gi 502304110  208 FSAWFEVFL-GGHWHTVDA 225
Cdd:pfam01841  90 AHAWVEVYLpGYGWVPVDP 108
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 167-225 1.70e-13

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: 63.94  E-value: 1.70e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304110   167 GVCRDFAHLAIALCRCMNIPARYCTGYL-GDIGVPIDPNPMDFSAWFEVFLGGHWHTVDA 225
Cdd:smart00460   7 GTCGEFAALFVALLRSLGIPARVVSGYLkAPDTIGGLRSIWEAHAWAEVYLEGGWVPVDP 66
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 113-226 3.04e-38

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 132.44  E-value: 3.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304110 113 TDRLADFAWARFSSTPLGWARVQAICDFVHDHITFDYLKADVLRTAHGGFTDKAGVCRDFAHLAIALCRCMNIPARYCTG 192
Cdd:COG1305   60 DPELRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSG 139

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502304110 193 YLGDIGVPIDPNPMDFSAWFEVFLGGH-WHTVDAR 226
Cdd:COG1305  140 YLPGEPPPGGGRADDAHAWVEVYLPGAgWVPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 133-225 3.03e-17

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: 75.13  E-value: 3.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304110  133 RVQAICDFVHDHITFDYLKA-----DVLRTahggFTDKAGVCRDFAHLAIALCRCMNIPARYCTGYLGDigvPIDPNPMD 207
Cdd:pfam01841  17 KARAIYDYVRKNITYDLPGRspgdgDAEEF----LFTGKGDCEDFASLFVALLRALGIPARYVTGYLRG---PDTVRGGD 89

                          90
                  ....*....|....*....
gi 502304110  208 FSAWFEVFL-GGHWHTVDA 225
Cdd:pfam01841  90 AHAWVEVYLpGYGWVPVDP 108
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 167-225 1.70e-13

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: 63.94  E-value: 1.70e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304110   167 GVCRDFAHLAIALCRCMNIPARYCTGYL-GDIGVPIDPNPMDFSAWFEVFLGGHWHTVDA 225
Cdd:smart00460   7 GTCGEFAALFVALLRSLGIPARVVSGYLkAPDTIGGLRSIWEAHAWAEVYLEGGWVPVDP 66
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 131-225 8.71e-11

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: 60.80  E-value: 8.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304110 131 WARVQAICDFVHDHITFDYLKAD----VLRTAHGGFTDKAGVCRDFAHLAIALCRCMNIPARYCTGYLGDIGVPIDPNpm 206
Cdd:COG5279  102 YEKVRAIHDWIVDNIEYDYEAYNsgksDSHSAYGALKNGKGVCEGYAKLFKLLCNKAGIECYIVTGYARGSGGESGNH-- 179

                         90
                 ....*....|....*....
gi 502304110 207 dfsAWFEVFLGGHWHTVDA 225
Cdd:COG5279  180 ---AWNAVKIDGKWYLVDA 195
DUF553 pfam04473
Transglutaminase-like domain; This family of uncharacterized archaeal proteins are related to ...
 136-197 1.42e-03

Transglutaminase-like domain; This family of uncharacterized archaeal proteins are related to Transglutaminase-like domains. This family has previously been called DUF553 and UPF0252.


Pssm-ID: 282345  Cd Length: 140  Bit Score: 38.20  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502304110  136 AICDFVHDHITFDYLKADVLRTAHGGFTD----------KAGVCRDFAHLAIALCRCMNiparYCTGYLGDI 197
Cdd:pfam04473  21 NILEWEDENIKYDYEKAELYPFLVLFLTYiqtpsetiktRKGVCSDYAILTAALLLDLN----VSPVYLVDV 88
 
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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