ID A0A1Q9CRD2_SYMMI Unreviewed; 3483 AA.
AC A0A1Q9CRD2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:OLP85471.1};
GN Name=HSP90 {ECO:0000313|EMBL:OLP85471.1};
GN ORFNames=AK812_SmicGene33536 {ECO:0000313|EMBL:OLP85471.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP85471.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP85471.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP85471.1,
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:OLP85471.1}.
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DR EMBL; LSRX01000975; OLP85471.1; -; Genomic_DNA.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; 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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR013103; RVT_2.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF07727; RVT_2; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00220; S_TKc; 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; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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:OLP85471.1}.
FT DOMAIN 1812..2103
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 376..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2881..2922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3443..3483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1756
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2897..2922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3469..3483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3483 AA; 391796 MW; DDDB70E55AC28738 CRC64;
MKKLGARIDL GKECVDLCSL KAAEVPLVQA QGGHPAVAVF PEGHSKAPKI PWSTVKDEGR
GPGIWHNDLG ETACAYMAAC SAVVCPEREA RPERLFYAKR LPPAIEDMLA HSTLNVETFL
GWWRGCKIQR DFWVERGDKL IRVHVVPRKY PSSPEGWQTE MSELKAELLR VLGGEVVEER
IPCRGPQLLS RESRSWKLQP ARAQPHALWI GRSVFQRHCE NTAANPNTSE VNVVMSKAAL
VSELAEYEVV AHPDWTINEV REMVKEQRTV RMSSEGQVPK GLAKMTLQQL MEEARKCGLV
LPEKPTKEVL TKLIRDAKAA PNDTVLSFGR YRGWAYNQVP VQYLDWALNE WHSSPNCSDD
LARLARWWEE KKSTKAGKLK VRGLPEDDPE KTATTPPPTN TTARQTGRAS SSRDPTEWIE
VYPETPGNRS PNGVQTLAAH AVIDENRLAG WDPEAAAIAG PDLMWAELPF GPWTPRRGRS
YKQHKEKKKS ERRLMRQVLE ALENQEHQVL YYKNAREDTK MKAILSGCAP PPGGDSGELT
AEEVFAKELQ ETGKRKRKGY HEAWAVEAEP PNIDEEPGDE PELREAGAKC ITFDQRVPKA
VQGALRKLHQ NLGHPPNSEL ARHIRLSGGS SEAVKDRTAK TLAETVRDHW VSWAGPPHTF
ALDLDSGFKS VFDEMCYEFG SFMSHAAGTA HWQHGMVERH NGAWKSIWER TVDSAMVVEH
EVAWTIAEVS NAKNQLRNKD GNSPRQWVFG ANPRLPGDVF DDENNLAAMS NYTVDARMQR
QNAIRQAARI AFMRVQTDQA MQRALLHRSR VKKTHYEPGD LVFIFRQKKP ERDKKPVKMW
VGPCTVIGNE GQNLWVSKGG RCLLCAPEHL RPAEAEEISE LLRVRAAMDD VQAIIDEDKA
LRDAFAPEDE ELIPDDGGNQ AEGKETDDIA EELLTGEGEA FQEKFVEMEN MDWDDGAERR
RRCLDDLPHW HSEEEKANAE QPMAQEVLFG KVASTQASRE KQMESEIPWS SIDPRDRPAF
LEAEQKQWSE HLKFEAVRVL TKEETEQVYA EVPPERILNS RFAYKDKARA QRAQHPDLPV
RAKARLCIGG HRDPDLGVRQ LSVDAPTACK DSLMLGMQCA VSHRWSASIG DVQAAFLNGV
AAPRGLFFKQ PPRGLPGVEE GVLVEIIKGV FGLSTSPRLW FEKLVQDIQN TEVKLEGTTL
HFEQNDIDPC VFHIVDARGD TVGLLETHVD DLLLLVEEKY KKATQEKLSQ TFPISEWEDD
AFKYVGSNYK KDGEGYQITQ EDYVEERLKF IEVPKGANQE QVDDRLFHDN RTAVGCLSWL
AKESRPDLAC AANFAQARQG SPTIADIKDT NKAIKQAKDY KENGIKIKPI PLHEMCLVVY
HDAAWGNSEP EDEAVAHLVG HRVGSQIGYL VLAVHNSGIG GRPCAMSTLA WKSHSCKRVC
RSTFAGETMA CCEGVECAIH LRARLLSLML RKLIKEPEAA EMIPIHAVTD CKSLFDFVHR
CGTPKPTADR RLIIDLASLK QIFLNEAKGW WKRERGDETP AVDDPLLLPF HWVPSGHQLS
DIMTKQMKPE AWWSAAGDSD VGLVRGGKSF WKSGISCTGC AGFSNCSFAP GEWVERESGT
AKLTPQDRTQ SSIILLVSAF RLSLECLPLL GLNMKRNVRR RQSQGTVRWT ARGMDGSGVY
LPPSVECSLA SDRGVDPLDK GGIAGFTSFT GFDNPTGKGF EKDKVDGYKE HETLDDDNQE
EAEDESSEDE NAEDANTPGD YPDNMSKDEA GTGEDPPLAR HPAPVSPAAA SVSGKIHRHL
KVKEKSPLGR FVRFNRKLGS GSYKTVWLGF DNDTGMEVAW NIISFQNLDK KAKKRISDEI
QMLKNLKHPK IIAFINAWTN KEQEKVCFIT ERVTGGSLLQ YIKRINAPLK LKVIRNWCRQ
ILEGLNYLHT RPDPIIHRDL KCDNIFINGN RGDIVIGDLG LSTTLRESCA VARSIVGTVD
FIAPEIYDEN YGTSVDIYAF GMVLLELRGD GVLAAGKVRE CSWLKGPPVR DDRKGAALER
MRQIYKKVLA GERPRNLRRV KDELLRSIVM QCSRMVRRQV FLSVRQKPDE RPTAQQLLDH
SWLEETDGPR NRLCELLPPE EAPDDVPDVD IFPKAAVAWT HHPGKKSTDA FHSLTSSHGE
PLCQLQPQLP QIMEEDEDLQ DGAALPLSQH PHSAVARFPF DVEPHHFLVK MHVLAFLLLP
TSFAALLSPS PSSECEASEA SLLQTASSMS CSPLPSITCD AQSGQMPRAH SKRQMRLVKD
LDPSIGLTPW NCSLCHNDAN AATVYGVERW DGLGQRAASL INFMALAAHL KLNFGGLLPN
PSEREHGVYI PKCMTQLFGT NYKELRRFAP EPHFDLCLFG PEAIQEAVNE KPWQKGQSIL
IEECGNGREF VDYLTSEFQE RLRQSTGLQR SGAFHFAGPA VKVAVHVRRG DLTNREHWAH
RNVADEIYMG LIQEVQDVLA ELGRTAEVHV FSSTEGGKFS SEDFDGYRSK KMQVHLNGKE
IDDWTHMTHA DVLIQAPSAF SWVPGVLNSK CVLAFDSYPK PLEDWIVHTQ GQLDSANKQH
LREQEDQTRL ADVLGKRQMQ QMSCQRQLSE KTDKDNEYPC LGREGSVDSH TDAAAHAVQE
EASKVDFVLP PEAETCGDFR HNSETAMAET FAFNADIQQL MSLIINTFYS NKEIFLRELI
SNASDALDKI RYESITDPDK IEAQPNFFIK IIPDKTNSTL TIEDSGIGMT KNELINNLGT
IAKSGTKAFM EAMAAGGDIS MIGQFGVGFY SAYLVSDKVR VVSKHNDDEQ YIWESGAGGS
FTVQKDTELV HGEIKRGTKI ICYLKEDQSE FLEERRLKDL VKKHSEFIGF PIELYVEKSK
EKEVTDSEEE EEEKKDEKEG DEPKIEEVDE EKEKEEKKKK TKKVKEVSHE WEQLNKNKPL
WMRKSEDVTN EEYASFYKSL SNDWEDHLAV KHFSVEGQLE FRALLFVPRR APFDLFETKK
KRNNIKLYVR RVFIMDDCEE LMPEWLNFVK GVVDSEDLPL NISRETLQQN KILRVIKKNL
VKKCLEMFAE IAEKKDDYKK FYEQFGKCLK LGVHEDSTNR TKVAELLRYH TSKSGDEQIS
LKEYVDRMKE GQNDIFYITG ESIAAVSSSP FLETLRKKGI EVLYMIDPID EYSVQQLKEF
DGKKLKSTTK EGLDIEDEDE KKKLEEMKAE FEPLTKLMKE VEKVIVSSRM ADSPCVLTTS
EYGWSANMER IMKAQALRDN SMTSYMVSKK TMEVNPKHSI MAELKKKAAA DKSDKTVKDL
IWLLFDTSLL TSGFNLDEPT QFAGRIHRMI KLGLSIDDDD EGLGDDDDLP PLEEVEGAAD
EASKMEEARA ARRVDRRWGA RSPEARADSV SFSQVGQNSE NLCQRILKSL VRGEVLAPPA
PTMGWALGCL GSCTIEVLLH GQPDVASPAS PRPMDTLEEP EPDPEDGEEQ ATAVDRAASR
LDS
//
