ID A0A2L2TML4_9HYPO Unreviewed; 700 AA.
AC A0A2L2TML4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI65877.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; LN649229; CEI65877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2TML4; -.
DR STRING; 56646.A0A2L2TML4; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000245910; Chromosome i.
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; PF02518; HATPase_c; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000245910}.
FT DOMAIN 25..180
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 211..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 517..552
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 227..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 79427 MW; FC8FB8AB9A004E02 CRC64;
MSETFEFQAE ISQLLSLIIN TVYSNKEIFL RELVSNASDA LDKIRYKSLA DPSQLESGKD
LRIDIIPDKA NKTLTIRDTG IGMTKADLVN NLGTIARSGT KQFMEALTAG ADVSMIGQFG
VGFYSAYLVA DRVTVISKNN DDEQYIWESS AGGTFSITED TDSEQLGRGT SIILHLKEEQ
TDYLNESKIK EVIKKHSEFI SYPIYLHVEK ETEKEVPDEE AEEVTEEGDD KKPKIEEVDD
DEEEKKPKTK KIKETKIEEE ELNKQKPIWT RNPQDISQEE YASFYKSLSN DWEDHLAVKH
FSVEGQLEFR AILFVPKRAP FDLFETKKTK NNIKLYVRRV FITDDATDLI PEWLGFVKGV
VDSEDLPLNL SRETLQQNKI MKVIKKNIVK KSLELFQEIA EDKEQFDKFY SAFSKNLKLG
IHEDSQNRSI LAKLLRFNST KSGDELTSLT DYVTRMPEHQ NNMYYITGES INAVSKSPFL
DALREKGFEV LFLVDPIDEY AMTQLKEFEG KKLVDITKDF ELEETEEEKK AREEEEKEYE
NLAKSLKNVL GDKVEKVVVS HKLGSSPCAI RTGQFGWSAN MERIMKAQAL RDTSMSSYMS
SKKTFEISPK SAIVQELKKK VENDGENDRT VKSIVQLLFE TSLLVSGFTI EEPAGFADRI
HKLVQLGLNI EEDDSAPADA DATDAPVAAA AGDSAMEEVD
//
