ID   HSP01_PSEMZ             Reviewed;          14 AA.
AC   P85904;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Putative heat shock protein 1 {ECO:0000303|PubMed:18602030};
DE   Flags: Fragment;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed in
RT   Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q31F72}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000255}.
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DR   PRIDE; P85904; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Stress response.
FT   CHAIN           <1..>14
FT                   /note="Putative heat shock protein 1"
FT                   /id="PRO_0000392518"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         14
FT                   /evidence="ECO:0000303|PubMed:18602030"
SQ   SEQUENCE   14 AA;  1531 MW;  8B5E93A77704CBB5 CRC64;
     ELVSNASDAL DKLR