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Conserved domains on  [gi|1002227444|ref|XP_015632051|]
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uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

trigger factor( domain architecture ID 1750330)

trigger factor functions as a peptidylprolyl isomerase that is involved in protein export and acts as a chaperone by maintaining the newly synthesized protein in an open conformation

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0006457|GO:0015031|GO:0043022|GO:0044183

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tig super family cl40800
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
 97-214 3.00e-10

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


The actual alignment was detected with superfamily member TIGR00115:

Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 59.11  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227444  97 VRVDLPGKATQKVFDEALTSLARDAPpVPGFRKSKggrtsnIPSSILLQMLGKSRVTKfVLQEILSITVGDFVKKENLKV 176
Cdd:TIGR00115   5 LTVEVPAEEVEEEVDKALKELAKTVK-IPGFRKGK------VPRSVVEKRYGESVLQE-ALNELLQEAFSEAVKEEKIRP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002227444 177 --NPEIKTTQSEEELESSFTpgssFSFSVVLQLEKPESDE 214
Cdd:TIGR00115  77 lgQPEIEVKELEDGKDLEFT----AEFEVYPEVELGDYKG 112
 
Name Accession Description Interval E-value
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
 97-214 3.00e-10

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 59.11  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227444  97 VRVDLPGKATQKVFDEALTSLARDAPpVPGFRKSKggrtsnIPSSILLQMLGKSRVTKfVLQEILSITVGDFVKKENLKV 176
Cdd:TIGR00115   5 LTVEVPAEEVEEEVDKALKELAKTVK-IPGFRKGK------VPRSVVEKRYGESVLQE-ALNELLQEAFSEAVKEEKIRP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002227444 177 --NPEIKTTQSEEELESSFTpgssFSFSVVLQLEKPESDE 214
Cdd:TIGR00115  77 lgQPEIEVKELEDGKDLEFT----AEFEVYPEVELGDYKG 112
Trigger_N pfam05697
Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly ...
 84-211 1.13e-09

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: 54.79  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227444  84 KTSVVSRDDETINVRVDLPGKATQKVFDEALTSLARDAPpVPGFRKSKggrtsnIPSSILLQMLGKSrVTKFVLQEILSI 163
Cdd:pfam05697   2 KVTVEKLEGLKVKLTVEVPAEEVEKAVDKALKKLAKKVN-IPGFRKGK------VPRSVIEKRYGKE-VYEEALNELLPE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002227444 164 TVGDFVKKENLKV--NPEIKTTQseeelessFTPGSSFSFSVVLQLeKPE 211
Cdd:pfam05697  74 AYEEAIEEEKLEPvgQPEIEVVE--------IEKGKDLEFTAEVEV-KPE 114
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 84-211 1.46e-08

FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 53.98  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227444  84 KTSVVSRDDETINVRVDLPGKATQKVFDEALTSLARDAPpVPGFRKSKggrtsnIPSSILLQMLGKSrVTKFVLQEILSI 163
Cdd:COG0544     2 KVTVEKLEGLKRKLTVEVPAEEVEKAVDKALKKLAKKVN-IPGFRKGK------VPRSVVEKRYGKE-VLEEALNELLPE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002227444 164 TVGDFVKKENLKV--NPEIKTTQSEEelessftpGSSFSFSVVLQLeKPE 211
Cdd:COG0544    74 AYEEAVEEEKLRPagQPEIDVVELEE--------GKDLEFTAEVEV-RPE 114
 
Name Accession Description Interval E-value
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
 97-214 3.00e-10

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 59.11  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227444  97 VRVDLPGKATQKVFDEALTSLARDAPpVPGFRKSKggrtsnIPSSILLQMLGKSRVTKfVLQEILSITVGDFVKKENLKV 176
Cdd:TIGR00115   5 LTVEVPAEEVEEEVDKALKELAKTVK-IPGFRKGK------VPRSVVEKRYGESVLQE-ALNELLQEAFSEAVKEEKIRP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002227444 177 --NPEIKTTQSEEELESSFTpgssFSFSVVLQLEKPESDE 214
Cdd:TIGR00115  77 lgQPEIEVKELEDGKDLEFT----AEFEVYPEVELGDYKG 112
Trigger_N pfam05697
Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly ...
 84-211 1.13e-09

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: 54.79  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227444  84 KTSVVSRDDETINVRVDLPGKATQKVFDEALTSLARDAPpVPGFRKSKggrtsnIPSSILLQMLGKSrVTKFVLQEILSI 163
Cdd:pfam05697   2 KVTVEKLEGLKVKLTVEVPAEEVEKAVDKALKKLAKKVN-IPGFRKGK------VPRSVIEKRYGKE-VYEEALNELLPE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002227444 164 TVGDFVKKENLKV--NPEIKTTQseeelessFTPGSSFSFSVVLQLeKPE 211
Cdd:pfam05697  74 AYEEAIEEEKLEPvgQPEIEVVE--------IEKGKDLEFTAEVEV-KPE 114
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 84-211 1.46e-08

FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 53.98  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002227444  84 KTSVVSRDDETINVRVDLPGKATQKVFDEALTSLARDAPpVPGFRKSKggrtsnIPSSILLQMLGKSrVTKFVLQEILSI 163
Cdd:COG0544     2 KVTVEKLEGLKRKLTVEVPAEEVEKAVDKALKKLAKKVN-IPGFRKGK------VPRSVVEKRYGKE-VLEEALNELLPE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002227444 164 TVGDFVKKENLKV--NPEIKTTQSEEelessftpGSSFSFSVVLQLeKPE 211
Cdd:COG0544    74 AYEEAVEEEKLRPagQPEIDVVELEE--------GKDLEFTAEVEV-RPE 114
 
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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