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Conserved domains on  [gi|1002298196|ref|XP_015612520|]
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uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

Trigger_N superfamily-containing protein( domain architecture ID 1005421)

Trigger_N superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trigger_N super family cl38195
Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly ...
 86-208 3.99e-07

Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly synthesized proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains. This family represents the N-terminal region of the protein.


The actual alignment was detected with superfamily member pfam05697:

Pssm-ID: 461717 [Multi-domain]  Cd Length: 144  Bit Score: 47.47  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298196  86 VSVQTEEDGLIKLRVTVADTMTESIFEKVFSKNVAAAQpLPGFRRmkgGKtrdIPKEIALHLIGPSkVKKETIKNIISLT 165
Cdd:pfam05697   3 VTVEKLEGLKVKLTVEVPAEEVEKAVDKALKKLAKKVN-IPGFRK---GK---VPRSVIEKRYGKE-VYEEALNELLPEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002298196 166 IAEYVQKEdldaskNLKVLQTYEELEAAFEPGKEFCFDATFHL 208
Cdd:pfam05697  75 YEEAIEEE------KLEPVGQPEIEVVEIEKGKDLEFTAEVEV 111
 
Name Accession Description Interval E-value
Trigger_N pfam05697
Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly ...
 86-208 3.99e-07

Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly synthesized proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains. This family represents the N-terminal region of the protein.


Pssm-ID: 461717 [Multi-domain]  Cd Length: 144  Bit Score: 47.47  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298196  86 VSVQTEEDGLIKLRVTVADTMTESIFEKVFSKNVAAAQpLPGFRRmkgGKtrdIPKEIALHLIGPSkVKKETIKNIISLT 165
Cdd:pfam05697   3 VTVEKLEGLKVKLTVEVPAEEVEKAVDKALKKLAKKVN-IPGFRK---GK---VPRSVIEKRYGKE-VYEEALNELLPEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002298196 166 IAEYVQKEdldaskNLKVLQTYEELEAAFEPGKEFCFDATFHL 208
Cdd:pfam05697  75 YEEAIEEE------KLEPVGQPEIEVVEIEKGKDLEFTAEVEV 111
 
Name Accession Description Interval E-value
Trigger_N pfam05697
Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly ...
 86-208 3.99e-07

Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly synthesized proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains. This family represents the N-terminal region of the protein.


Pssm-ID: 461717 [Multi-domain]  Cd Length: 144  Bit Score: 47.47  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298196  86 VSVQTEEDGLIKLRVTVADTMTESIFEKVFSKNVAAAQpLPGFRRmkgGKtrdIPKEIALHLIGPSkVKKETIKNIISLT 165
Cdd:pfam05697   3 VTVEKLEGLKVKLTVEVPAEEVEKAVDKALKKLAKKVN-IPGFRK---GK---VPRSVIEKRYGKE-VYEEALNELLPEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002298196 166 IAEYVQKEdldaskNLKVLQTYEELEAAFEPGKEFCFDATFHL 208
Cdd:pfam05697  75 YEEAIEEE------KLEPVGQPEIEVVEIEKGKDLEFTAEVEV 111
 
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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