ID K9FZP1_PEND2 Unreviewed; 697 AA.
AC K9FZP1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:EKV14057.1};
GN ORFNames=PDIG_35400 {ECO:0000313|EMBL:EKV14057.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV14057.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKV14057.1}.
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DR EMBL; AKCT01000147; EKV14057.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FZP1; -.
DR STRING; 1170229.K9FZP1; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; K9FZP1; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
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 PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 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 Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW Stress response {ECO:0000313|EMBL:EKV14057.1}.
FT DOMAIN 25..180
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 215..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 79562 MW; 92CA4525C6FD183C CRC64;
MSETFEFQAE ISQLLSLIIN TVYSNKEIFL RELISNASDA LDKIRYEALS DPSKLDSNKD
LRIDIIPDLE NKTLTIRDTG IGMTKADLIN NLGTIARSGT KQFMEALSAG ADISMIGQFG
VGFYSAYLVA DRVTFVSKHN DDEQYIWESA AGGTFTLKED TEGEQLGRGS KIILHLKDEQ
MDYLNEARIK EVVRKHSEFI SYPIYLHVLK ETETEVPDEE AEEIKEDDEK KPKVEEVDDE
EEEKKEKKTK TVKESKIEEE ELNKTKPIWT RNPADITTEE YASFYKSLSN DWEDHLGVKH
FSVEGQLEFR AILFVPKRAP FDLFETKKTK NNIKLYVRRV FITDDATDLI PEWLSFVKGV
VDSEDLPLNL SRETLQQNKI MKVIKKNIVK KILELFVEIS EDREQFDKFY QAFSKNIKLG
IHEDAQNRPT LAKLLRYQST KSGDEQTSLA DYITRMPEHQ KNMYYITGES IKAVANSPFL
DTLKQKNFEV LFLVDPIDEY AFTQLKEYDG KKLVDITKDF ELEETEEEKT QRETEEKEFE
DLAKALKNVL GDKVEKVVVS SKLVGSPCAI RTGQFGWSAN MERIMKAQAL RDTSMSSYMS
SKKTFEISPK SPIIKELKKK VEADGENDRT VKSITQLLFE TSLLVSGFTI EEPASFSERI
HKLVSLGLNI DEDEAAPATE AAAPAEATGE STMEEVD
//
