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Conserved domains on  [gi|388856964|emb|CCF49384|]
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related to ROT1-molecular chaperone in the endoplasmic reticulum [Ustilago hordei]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rot1 super family cl24235
Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an ...
 30-198 5.50e-42

Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an essential molecular chaperone in the endoplasmic reticulum. Molecular chaperones transiently interact with unfolded proteins to inhibit their self-aggregation and to support their folding and/or assembly. Rot1 is a general chaperone with some substrate specificity, its substrates being the structurally unrelated Kre5 Kre6 Big1 Atg22, which are type I, type II, and polytopic membrane proteins. The dependencies of each for Rot1 do not share similarities. However, their folding does require BiP, and one of these proteins was simultaneously associated with both Rot1 and BiP. In addition, Rot1 may cooperate with BiP/Kar2 in the folding of Kre6.


The actual alignment was detected with superfamily member pfam10681:

Pssm-ID: 431433  Cd Length: 209  Bit Score: 140.76  E-value: 5.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856964   30 LQGTWSTGSGAVRTGPGFWNPRTQQFTVPPTAGRSFSFTKDGFWEEAMFQWSNDPTLPECVSATLLWQHGNYSFNPiNGT 109
Cdd:pfam10681   1 LVGTWSSKSNQVFTGPGFYDPVDELLIEPSLPGISYSFTEDGYFEEAYYRAISNPTNPSCPKAIMQWQHGTYELLD-NGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856964  110 LRMDPFWGDGFQTQWIGCDATSSATSNntaapvasYNQVYLYDPPAVSIDSHYGVssYKLEMAQLSGELLNPMWKVLNPP 189
Cdd:pfam10681  80 LVLTPIAVDGRQLLSDPCAGGTSTYTR--------YNQTELFKSYEVSVDPYHGR--YRLQLYQFDGSPMQPLYLAYRPP 149


                  ....*....
gi 388856964  190 SMLPTDVLH 198
Cdd:pfam10681 150 QMLPTTTLN 158
 
Name Accession Description Interval E-value
Rot1 pfam10681
Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an ...
 30-198 5.50e-42

Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an essential molecular chaperone in the endoplasmic reticulum. Molecular chaperones transiently interact with unfolded proteins to inhibit their self-aggregation and to support their folding and/or assembly. Rot1 is a general chaperone with some substrate specificity, its substrates being the structurally unrelated Kre5 Kre6 Big1 Atg22, which are type I, type II, and polytopic membrane proteins. The dependencies of each for Rot1 do not share similarities. However, their folding does require BiP, and one of these proteins was simultaneously associated with both Rot1 and BiP. In addition, Rot1 may cooperate with BiP/Kar2 in the folding of Kre6.


Pssm-ID: 431433  Cd Length: 209  Bit Score: 140.76  E-value: 5.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856964   30 LQGTWSTGSGAVRTGPGFWNPRTQQFTVPPTAGRSFSFTKDGFWEEAMFQWSNDPTLPECVSATLLWQHGNYSFNPiNGT 109
Cdd:pfam10681   1 LVGTWSSKSNQVFTGPGFYDPVDELLIEPSLPGISYSFTEDGYFEEAYYRAISNPTNPSCPKAIMQWQHGTYELLD-NGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856964  110 LRMDPFWGDGFQTQWIGCDATSSATSNntaapvasYNQVYLYDPPAVSIDSHYGVssYKLEMAQLSGELLNPMWKVLNPP 189
Cdd:pfam10681  80 LVLTPIAVDGRQLLSDPCAGGTSTYTR--------YNQTELFKSYEVSVDPYHGR--YRLQLYQFDGSPMQPLYLAYRPP 149


                  ....*....
gi 388856964  190 SMLPTDVLH 198
Cdd:pfam10681 150 QMLPTTTLN 158
 
Name Accession Description Interval E-value
Rot1 pfam10681
Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an ...
 30-198 5.50e-42

Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an essential molecular chaperone in the endoplasmic reticulum. Molecular chaperones transiently interact with unfolded proteins to inhibit their self-aggregation and to support their folding and/or assembly. Rot1 is a general chaperone with some substrate specificity, its substrates being the structurally unrelated Kre5 Kre6 Big1 Atg22, which are type I, type II, and polytopic membrane proteins. The dependencies of each for Rot1 do not share similarities. However, their folding does require BiP, and one of these proteins was simultaneously associated with both Rot1 and BiP. In addition, Rot1 may cooperate with BiP/Kar2 in the folding of Kre6.


Pssm-ID: 431433  Cd Length: 209  Bit Score: 140.76  E-value: 5.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856964   30 LQGTWSTGSGAVRTGPGFWNPRTQQFTVPPTAGRSFSFTKDGFWEEAMFQWSNDPTLPECVSATLLWQHGNYSFNPiNGT 109
Cdd:pfam10681   1 LVGTWSSKSNQVFTGPGFYDPVDELLIEPSLPGISYSFTEDGYFEEAYYRAISNPTNPSCPKAIMQWQHGTYELLD-NGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856964  110 LRMDPFWGDGFQTQWIGCDATSSATSNntaapvasYNQVYLYDPPAVSIDSHYGVssYKLEMAQLSGELLNPMWKVLNPP 189
Cdd:pfam10681  80 LVLTPIAVDGRQLLSDPCAGGTSTYTR--------YNQTELFKSYEVSVDPYHGR--YRLQLYQFDGSPMQPLYLAYRPP 149


                  ....*....
gi 388856964  190 SMLPTDVLH 198
Cdd:pfam10681 150 QMLPTTTLN 158
 
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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