ID A0A3S3MCF2_9MAGN Unreviewed; 801 AA.
AC A0A3S3MCF2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Heat shock protein 90-6, mitochondrial isoform X3 {ECO:0000313|EMBL:RWR73862.1};
GN ORFNames=CKAN_00216900 {ECO:0000313|EMBL:RWR73862.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR73862.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR73862.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR73862.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
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:RWR73862.1}.
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DR EMBL; QPKB01000001; RWR73862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3MCF2; -.
DR STRING; 337451.A0A3S3MCF2; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
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; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR PANTHER; PTHR11528:SF41; HEAT SHOCK PROTEIN 90-6, MITOCHONDRIAL; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000283530};
KW Stress response {ECO:0000313|EMBL:RWR73862.1}.
FT DOMAIN 116..278
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 90453 MW; F9CDD78AF4ACB11B CRC64;
MQRLSRRSVS AILRTGGATS RTSAPPPLPV LHDSSEGGDS HHSKFASRLY SVLIPVKQSA
SDSAKHPNLR NGLLAFNRYE STAAATDSSL PPEEKFEYQA EVSRLMDLIV HSLYSNKEVF
LRELISNASD ALDKLRFLSV TEPALLKDAA DLDIRIQTDQ DNGIITLTDT GIGMTREELV
DCLGTIAQSG TAKFLKAVKE SKESGADSNL IGQFGVGFYS AFLVSDKVMV STKSPKSDKQ
YVWEGEANAS SYTIREETDP EKLIPRGTRI TLFLKRDDKG FAHPERVQNL VKNYSQFVSF
PIYTWQEKGF TKEVEVDEDP AEGKKDEENE TKTEKKKKTK KVVEKYWEWE LTNETQPIWL
RNPKEVSTEE YNEFYKKTFN EYLDPLASSH FTTEGEVEFR SILFVPAMSP MGKEDISNPK
TKNIKLYVKR VFISDDFDGE LFPRYLSFVK GVVDSNDLPL NVSREILQES RIVRIMRKRL
VRKAFDMILG ISLSENKDDY DKFWENFGKH LKLGCLEDHQ NHKRIAPLLR FSSSQSEEEL
ISLDEYLENM KPEQKDIYYI AADSLKSARN APSLEMLLEK DFEVLFLIDP IDEVAIQNLK
SYKEKNFVDI SKEDLDLGDK DEEKEKEIKQ EFGKTCDWIK KRLGDKVASV QISSRLSTSP
CVLVSGKFGW SANMERLMKA QTMGDTSSLE FMRGRRVFEI NPRHPIIKDL NDACSRSPDN
PEALRAIDLL YDTALISSGF TPENPTDLGG KIYEMMGMAL AGKWTAPGTT GQRATDPQPG
VSGDQEAVEA EVVGPSEAGQ K
//
