ID   V9P9I3_9BILA            Unreviewed;       282 AA.
AC   V9P9I3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:AGW23669.1};
DE   Flags: Fragment;
OS   Meloidogyne naasi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=244176 {ECO:0000313|EMBL:AGW23669.1};
RN   [1] {ECO:0000313|EMBL:AGW23669.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30708461; DOI=.1094/PDIS-03-13-0263-RE;
RA   Nischwitz C., Skantar A., Handoo Z.A., Hult M.N., Schmitt M.E.,
RA   McClure M.A.;
RT   "Occurrence of Meloidogyne fallax in North America, and Molecular
RT   Characterization of M. fallax and M. minor from U.S. Golf Course Greens.";
RL   Plant Dis. 97:1424-1430(2013).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; KC262248; AGW23669.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9P9I3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Stress response {ECO:0000313|EMBL:AGW23669.1}.
FT   REGION          134..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGW23669.1"
FT   NON_TER         282
FT                   /evidence="ECO:0000313|EMBL:AGW23669.1"
SQ   SEQUENCE   282 AA;  32592 MW;  DF8818C460BA4C97 CRC64;
     TGIGMTKADL VNNLGTIAKS DTKAFMEALQ AGADISMIGQ FGVGFYSAFL VADRVTVTSK
     HNDDDCHQWE SSAGGSFIIR NCVDPELTRG TKITLYLKED QTDYLEERRI REVVKKHSQF
     IGYPIKLLVE KERDKEISDD EAEEENKDLK KEPKEEGDKE MKEADKEAEE GGEEKEKEGE
     KKKKTKKIKE KYTEDEELNK TKPIWTRNPD DITNEEYAEF YKSLSNDWED HLAVKHLSVE
     GQLEFRALLF VPQRAPFDMF ENKKQKNAIK LYVRRVFIME NC
//