ID A3E4E3_KARVE Unreviewed; 709 AA.
AC A3E4E3;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ABI14419.1};
OS Karlodinium veneficum (Dinoflagellate) (Karlodinium micrum).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Gymnodiniales; Kareniaceae;
OC Karlodinium.
OX NCBI_TaxID=407301 {ECO:0000313|EMBL:ABI14419.1};
RN [1] {ECO:0000313|EMBL:ABI14419.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17360573; DOI=10.1073/pnas.0700258104;
RA Zhang H., Hou Y., Miranda L., Campbell D.A., Sturm N.R., Gaasterland T.,
RA Lin S.;
RT "Spliced leader RNA trans-splicing in dinoflagellates.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4618-4623(2007).
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; DQ884433; ABI14419.1; -; mRNA.
DR AlphaFoldDB; A3E4E3; -.
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; 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 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 2: Evidence at transcript level;
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:ABI14419.1}.
FT REGION 215..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..695
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 81569 MW; 3B6807897A413CEB CRC64;
MAETFAFNAD IQQLMSLIIN TFYSNKEIFL RELVSNASDA LDKIRYESIT DPEKIEAQPN
FYIKIIPDKT NSTITIEDSG IGMTKNELIN NLGTIAKSGT KAFMEAMAAG GDISMIGQFG
VGFYSAYLGS DKVRVISKHN DDEQYVWESA AGGSFTVQKD TEMVHGEVKR GTKVICYLKE
DQSEFLEERR LKDLVKKHSE FIGFPIELYV EKSKEKEVTD SEEDEEEKKE EDKEGDEPKI
EEVDEEKEKE EKKKKMKKVK EVSHEWEQLN KNKPLWMRKS EDVTNEEYAA FYKSLSNDWE
DHLAVKHFSV EGQLEFRALL FVPRRAPFDM FESKKKRTNI KLYVRRVFIM DDCDELMPEW
LSFVKGVVDS EDLPLNISRE TLQQNKILRV IKKNLVKKCL EMFAEISEKK DDYKKFYEQF
SKNIKLGIHE DSTNRAKVAE LLRYHTSKSG DEQISFKEYV DRMKEGQNDI YYITGESIAA
VSSSPFLETL RKKGLEVLYM VDPVDEYAVQ QLKEFDGKKL KSTTKEGLDI EDEDEKKKIE
ELKAEFEPLT KLMKEVLGDK VEKVLISSRM ADSPCVLTTS EYGWSANMER IMKAQALRDN
SMTSYMVSKK TMEVNPKHSI MTELKKKAAA DKSDKTVKDL IWLLFDTSLL TSGFNLDEPT
QFAGRIHRMI KLGLSIDDDD EGLGDDDDLP PLEEVEGAAD EASKMEEVD
//
