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Conserved domains on  [gi|584368480|gb|EWG88449|]
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Png1p [Saccharomyces cerevisiae P301]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 183-237 6.35e-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: 63.17  E-value: 6.35e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584368480   183 LLETRKGRCGEWCNLFTLILKSFGLDVRYVWN--------------REDHVWCEYFSNflNRWVHVDSC 237
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGylkapdtigglrsiWEAHAWAEVYLE--GGWVPVDPT 67
Rad4 super family cl44506
Rad4 transglutaminase-like domain;
220-274 2.04e-05

Rad4 transglutaminase-like domain;


The actual alignment was detected with superfamily member pfam03835:

Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 43.93  E-value: 2.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584368480  220 WCEYFSNFLNRWVHVDSC-------EQSFDQPYIYSINWnkKMSYCIAFGKDGVV-DVSKRYI 274
Cdd:pfam03835  39 WVEVFNPETKKWISVDPLvlktielKSKFEPRIAEKALN--VMTYVVAFDSDGGAkDVTRRYC 99
 
Name Accession Description Interval E-value
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 183-237 6.35e-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: 63.17  E-value: 6.35e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584368480   183 LLETRKGRCGEWCNLFTLILKSFGLDVRYVWN--------------REDHVWCEYFSNflNRWVHVDSC 237
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGylkapdtigglrsiWEAHAWAEVYLE--GGWVPVDPT 67
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 167-235 9.62e-12

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: 61.27  E-value: 9.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584368480  167 RCGNITRFPRYNDPIKLLETRKGRCGEWCNLFTLILKSFGLDVRYVWNRED----------HVWCE-YFSNflNRWVHVD 235
Cdd:pfam01841  30 TYDLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRgpdtvrggdaHAWVEvYLPG--YGWVPVD 107
Rad4 pfam03835
Rad4 transglutaminase-like domain;
220-274 2.04e-05

Rad4 transglutaminase-like domain;


Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 43.93  E-value: 2.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584368480  220 WCEYFSNFLNRWVHVDSC-------EQSFDQPYIYSINWnkKMSYCIAFGKDGVV-DVSKRYI 274
Cdd:pfam03835  39 WVEVFNPETKKWISVDPLvlktielKSKFEPRIAEKALN--VMTYVVAFDSDGGAkDVTRRYC 99
 
Name Accession Description Interval E-value
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 183-237 6.35e-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: 63.17  E-value: 6.35e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584368480   183 LLETRKGRCGEWCNLFTLILKSFGLDVRYVWN--------------REDHVWCEYFSNflNRWVHVDSC 237
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGylkapdtigglrsiWEAHAWAEVYLE--GGWVPVDPT 67
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 167-235 9.62e-12

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: 61.27  E-value: 9.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584368480  167 RCGNITRFPRYNDPIKLLETRKGRCGEWCNLFTLILKSFGLDVRYVWNRED----------HVWCE-YFSNflNRWVHVD 235
Cdd:pfam01841  30 TYDLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRgpdtvrggdaHAWVEvYLPG--YGWVPVD 107
Rad4 pfam03835
Rad4 transglutaminase-like domain;
220-274 2.04e-05

Rad4 transglutaminase-like domain;


Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 43.93  E-value: 2.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584368480  220 WCEYFSNFLNRWVHVDSC-------EQSFDQPYIYSINWnkKMSYCIAFGKDGVV-DVSKRYI 274
Cdd:pfam03835  39 WVEVFNPETKKWISVDPLvlktielKSKFEPRIAEKALN--VMTYVVAFDSDGGAkDVTRRYC 99
 
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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