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Conserved domains on  [gi|1582520279|gb|TBD01072|]
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transglutaminase family protein [Rhizobium ruizarguesonis]

Protein Classification

transglutaminase family protein( domain architecture ID 12090973)

transglutaminase family protein may act as a cysteine protease

CATH:  3.10.620.30|2.60.40.2250

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, ...
 112-220 7.18e-39

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


:

Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 133.98  E-value: 7.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582520279 112 KLVKELIKGigGDNELARMHALMAAIHETVDYKPGTSNTETTAEQALEKKSGVCQDHAHIFIAAARALQVPARYISGYLM 191
Cdd:COG1305    65 ALAAELTGG--ATTPYEKARALYDWVRDNIRYDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSGYLP 142

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1582520279 192 ME---EKIEQAATHAWAEAHIPGLGWVGFDPA 220
Cdd:COG1305   143 GEpppGGGRADDAHAWVEVYLPGAGWVPFDPT 174
Bact_transglu_N pfam08379
Bacterial transglutaminase-like N-terminal region; This region is found towards the N-terminus ...
 3-81 6.80e-21

Bacterial transglutaminase-like N-terminal region; This region is found towards the N-terminus of various archaeal and bacterial hypothetical proteins. Some of these are annotated as being transglutaminase-like proteins, and in fact contain a transglutaminase-like superfamily domain (pfam01841).


:

Pssm-ID: 462455  Cd Length: 80  Bit Score: 84.13  E-value: 6.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582520279   3 LKISHLTEYRYDGPTQFSLQRLRLTPPTSPAQKVLGWALNVEGATPEV-EYDDQYGNHVNLVSLEGEQDVTRILAEGEVE 81
Cdd:pfam08379   1 YRIRHRTRYRYDEPVSLSPHRLRLRPRSHPGQRVLSYSLDISPEPAARrWRRDAFGNRVARFSFDEPHTELVITAESEVE 80
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 112-220 7.18e-39

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 133.98  E-value: 7.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582520279 112 KLVKELIKGigGDNELARMHALMAAIHETVDYKPGTSNTETTAEQALEKKSGVCQDHAHIFIAAARALQVPARYISGYLM 191
Cdd:COG1305    65 ALAAELTGG--ATTPYEKARALYDWVRDNIRYDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSGYLP 142

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1582520279 192 ME---EKIEQAATHAWAEAHIPGLGWVGFDPA 220
Cdd:COG1305   143 GEpppGGGRADDAHAWVEVYLPGAGWVPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 122-219 3.60e-28

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: 104.02  E-value: 3.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582520279 122 GGDNELARMHALMAAIHETVDYK-PGTSNTETTAEQALEKKSGVCQDHAHIFIAAARALQVPARYISGYLMMEEKIEQAA 200
Cdd:pfam01841  10 GATDPLEKARAIYDYVRKNITYDlPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRGGD 89

                          90
                  ....*....|....*....
gi 1582520279 201 THAWAEAHIPGLGWVGFDP 219
Cdd:pfam01841  90 AHAWVEVYLPGYGWVPVDP 108
Bact_transglu_N pfam08379
Bacterial transglutaminase-like N-terminal region; This region is found towards the N-terminus ...
 3-81 6.80e-21

Bacterial transglutaminase-like N-terminal region; This region is found towards the N-terminus of various archaeal and bacterial hypothetical proteins. Some of these are annotated as being transglutaminase-like proteins, and in fact contain a transglutaminase-like superfamily domain (pfam01841).


Pssm-ID: 462455  Cd Length: 80  Bit Score: 84.13  E-value: 6.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582520279   3 LKISHLTEYRYDGPTQFSLQRLRLTPPTSPAQKVLGWALNVEGATPEV-EYDDQYGNHVNLVSLEGEQDVTRILAEGEVE 81
Cdd:pfam08379   1 YRIRHRTRYRYDEPVSLSPHRLRLRPRSHPGQRVLSYSLDISPEPAARrWRRDAFGNRVARFSFDEPHTELVITAESEVE 80
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 157-221 2.19e-15

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: 68.95  E-value: 2.19e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582520279  157 ALEKKSGVCQDHAHIFIAAARALQVPARYISGYLMMEEKIEQAAT----HAWAEAHIPGlGWVGFDPAN 221
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRSiweaHAWAEVYLEG-GWVPVDPTP 68
 
Name Accession Description Interval E-value
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 112-220 7.18e-39

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


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 133.98  E-value: 7.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582520279 112 KLVKELIKGigGDNELARMHALMAAIHETVDYKPGTSNTETTAEQALEKKSGVCQDHAHIFIAAARALQVPARYISGYLM 191
Cdd:COG1305    65 ALAAELTGG--ATTPYEKARALYDWVRDNIRYDPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSGYLP 142

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1582520279 192 ME---EKIEQAATHAWAEAHIPGLGWVGFDPA 220
Cdd:COG1305   143 GEpppGGGRADDAHAWVEVYLPGAGWVPFDPT 174
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 122-219 3.60e-28

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: 104.02  E-value: 3.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582520279 122 GGDNELARMHALMAAIHETVDYK-PGTSNTETTAEQALEKKSGVCQDHAHIFIAAARALQVPARYISGYLMMEEKIEQAA 200
Cdd:pfam01841  10 GATDPLEKARAIYDYVRKNITYDlPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDTVRGGD 89

                          90
                  ....*....|....*....
gi 1582520279 201 THAWAEAHIPGLGWVGFDP 219
Cdd:pfam01841  90 AHAWVEVYLPGYGWVPVDP 108
Bact_transglu_N pfam08379
Bacterial transglutaminase-like N-terminal region; This region is found towards the N-terminus ...
 3-81 6.80e-21

Bacterial transglutaminase-like N-terminal region; This region is found towards the N-terminus of various archaeal and bacterial hypothetical proteins. Some of these are annotated as being transglutaminase-like proteins, and in fact contain a transglutaminase-like superfamily domain (pfam01841).


Pssm-ID: 462455  Cd Length: 80  Bit Score: 84.13  E-value: 6.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582520279   3 LKISHLTEYRYDGPTQFSLQRLRLTPPTSPAQKVLGWALNVEGATPEV-EYDDQYGNHVNLVSLEGEQDVTRILAEGEVE 81
Cdd:pfam08379   1 YRIRHRTRYRYDEPVSLSPHRLRLRPRSHPGQRVLSYSLDISPEPAARrWRRDAFGNRVARFSFDEPHTELVITAESEVE 80
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 157-221 2.19e-15

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: 68.95  E-value: 2.19e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582520279  157 ALEKKSGVCQDHAHIFIAAARALQVPARYISGYLMMEEKIEQAAT----HAWAEAHIPGlGWVGFDPAN 221
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRSiweaHAWAEVYLEG-GWVPVDPTP 68
 
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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