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Conserved domains on  [gi|74635734|sp|Q6CFU5|]
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RecName: Full=Protein ROT1; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rot1 pfam10681
Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an ...
 31-245 6.52e-132

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: 370.72  E-value: 6.52e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74635734    31 LEGTWSSKSGAVITGPDFYDPIDELLLEPTLPGISYSFTKDGFFEEAIYQVSANPKDPKCPTGVLIFQHGTYNISDNGTL 110
Cdd:pfam10681   1 LVGTWSSKSNQVFTGPGFYDPVDELLIEPSLPGISYSFTEDGYFEEAYYRAISNPTNPSCPKAIMQWQHGTYELLDNGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74635734   111 TLEPYMVDGRQLLSDPCKqEENAVYSRYNQTEKFKRFSVYVDPYHGRYRLDLFQFNGAPMPPMYLAYRPAMMLPTVTLNP 190
Cdd:pfam10681  81 VLTPIAVDGRQLLSDPCA-GGTSTYTRYNQTELFKSYEVSVDPYHGRYRLQLYQFDGSPMQPLYLAYRPPQMLPTTTLNP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 74635734   191 TQEASqpentgstrAKIRRSIDN----RKVTGIKKHSVVDYNSLWWFGVSMIAAGGAGW 245
Cdd:pfam10681 160 TDTAT---------AKVKRSLGSenplNTNAVKKRRSLINADRWWWVGVGMTGVGGLAF 209
 
Name Accession Description Interval E-value
Rot1 pfam10681
Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an ...
 31-245 6.52e-132

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: 370.72  E-value: 6.52e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74635734    31 LEGTWSSKSGAVITGPDFYDPIDELLLEPTLPGISYSFTKDGFFEEAIYQVSANPKDPKCPTGVLIFQHGTYNISDNGTL 110
Cdd:pfam10681   1 LVGTWSSKSNQVFTGPGFYDPVDELLIEPSLPGISYSFTEDGYFEEAYYRAISNPTNPSCPKAIMQWQHGTYELLDNGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74635734   111 TLEPYMVDGRQLLSDPCKqEENAVYSRYNQTEKFKRFSVYVDPYHGRYRLDLFQFNGAPMPPMYLAYRPAMMLPTVTLNP 190
Cdd:pfam10681  81 VLTPIAVDGRQLLSDPCA-GGTSTYTRYNQTELFKSYEVSVDPYHGRYRLQLYQFDGSPMQPLYLAYRPPQMLPTTTLNP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 74635734   191 TQEASqpentgstrAKIRRSIDN----RKVTGIKKHSVVDYNSLWWFGVSMIAAGGAGW 245
Cdd:pfam10681 160 TDTAT---------AKVKRSLGSenplNTNAVKKRRSLINADRWWWVGVGMTGVGGLAF 209
 
Name Accession Description Interval E-value
Rot1 pfam10681
Chaperone for protein-folding within the ER, fungal; This conserved fungal family is an ...
 31-245 6.52e-132

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: 370.72  E-value: 6.52e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74635734    31 LEGTWSSKSGAVITGPDFYDPIDELLLEPTLPGISYSFTKDGFFEEAIYQVSANPKDPKCPTGVLIFQHGTYNISDNGTL 110
Cdd:pfam10681   1 LVGTWSSKSNQVFTGPGFYDPVDELLIEPSLPGISYSFTEDGYFEEAYYRAISNPTNPSCPKAIMQWQHGTYELLDNGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74635734   111 TLEPYMVDGRQLLSDPCKqEENAVYSRYNQTEKFKRFSVYVDPYHGRYRLDLFQFNGAPMPPMYLAYRPAMMLPTVTLNP 190
Cdd:pfam10681  81 VLTPIAVDGRQLLSDPCA-GGTSTYTRYNQTELFKSYEVSVDPYHGRYRLQLYQFDGSPMQPLYLAYRPPQMLPTTTLNP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 74635734   191 TQEASqpentgstrAKIRRSIDN----RKVTGIKKHSVVDYNSLWWFGVSMIAAGGAGW 245
Cdd:pfam10681 160 TDTAT---------AKVKRSLGSenplNTNAVKKRRSLINADRWWWVGVGMTGVGGLAF 209
 
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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