ID A0A1Q9EI86_SYMMI Unreviewed; 1215 AA.
AC A0A1Q9EI86;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:OLQ07142.1};
GN ORFNames=AK812_SmicGene9503 {ECO:0000313|EMBL:OLQ07142.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ07142.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ07142.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ07142.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) 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}.
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:OLQ07142.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSRX01000146; OLQ07142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9EI86; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000186817; 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; cd06661; GGCT_like; 1.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR009288; AIG2-like_dom.
DR InterPro; IPR013024; GGCT-like.
DR InterPro; IPR036568; GGCT-like_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF06094; GGACT; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; 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; SSF110857; Gamma-glutamyl cyclotransferase-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF48452; TPR-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:UP000186817};
KW Stress response {ECO:0000313|EMBL:OLQ07142.1}.
FT DOMAIN 269..426
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 135544 MW; AFD2F8EFEB7FC61F CRC64;
MAARPPAAKR GASPKKVAAV PKTKAAPKEK AAEKAASAKD LVHAVFAYGT LRGDFEDTGD
HWGVIERTGA AWLRTSVTGF KLFQEDRAFY PFAVQSDEEQ DRLHGTILIW PAGDVSRKAI
ETCDRIEGFD PEHPNDGLYC RALVDAPVPL EALKAKMKEQ PWLKQELEGL DQKALDQEHI
SVRAFVYHQP MGDKADCSKA FPGGDWLESR LKDLESKFHG GSQKRNKKAS FHSSLALQAA
MAPAELETYA FNADISQLMS LIINAFYTNK EIFLRELISN ASDALDKIQF QASKDPSKLD
AEPNLYIKVT PDKDAGMVTV EDTGIGMTRE EMILHLGTIA KSGTKAFMEA VSSGADMSMI
GQFGVGFYSS YLVSEKVRVV SKSNDDEQYV WESTAGGTFL IWKDTKFEHG VLKRGTKVIC
YLKEDQAEFL ESDRLKELIM KHSAFVGFPI DLRMEHRQEE DIEVEEEGVE APEKRRKVTV
SYSWELINKN KPLWLRPASE VSHEEYAELY KFLSGDWEDH LAVKHVMQSG QVDFKALLYC
PTTAPKDMFD MGKMSQRFSI RLYVRRVFIK EFNDLIPKWM GFVKGIVDSD DMPLNISREM
LQQNAILKHI KTGLQKNIFS MFEELSADKA RFKAFHEAFS QCLKLGVYED HANREQIVPL
LRYHSSKSGE EMVGFDEYIA RMKPGQRHIL YITGRTKRDA ARSPYIEGLK RDGYEVIYMT
DPVDEYAVQF LKEYRGYEVL SCMSMDAARL LDHRSEADLK AELEPLRKRL QELLAEGGPS
SVTLASLNPE CCAQLASSEQ GTVLELNFKH SFVKELGKHT VLSQGAQQPS EEHLALSLCR
LLQDMAALEG TDADDPARAD TCEKCQDLIQ ALNAGEADAS GELPSLGAAS VAREAARERL
ETSEGKADGS ANLLSCGRRV RVVRGERARR AMISFVDEDA KTVDVLYPQP AASGKQEDEE
EGVPAKYVQA LQDFELTTVP SEDSLFKSAT ADKERGNQLF KLKDYEAASE FYGTALARFA
ARPVGRGEQV LLRRQDHDKE GKSALALATV LSVDSEGLCE LSNGAELPAG ELLPVCQELL
PLHTSLYMNR ARCRQNLGRH AEASQDLSAV LGLWQAVDKR MLQADPEMKE AELKGLYTAE
YLRARSRLAR GLSRSAAQDV KDALARSPPA ATVKQLKQLK TEVQAAQEKH RQVNSPLAKE
LAKLMISLRG GPQIS
//