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Database: UniProt
Entry: A5AHA8_VITVI
LinkDB: A5AHA8_VITVI
Original site: A5AHA8_VITVI 
ID   A5AHA8_VITVI            Unreviewed;       699 AA.
AC   A5AHA8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN   ORFNames=VITISV_029391 {ECO:0000313|EMBL:CAN62488.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN62488.1};
RN   [1] {ECO:0000313|EMBL:CAN62488.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT   vinifera L.): coping with a highly heterozygous genome.";
RL   PLoS ONE 2:e1326-e1326(2007).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; AM426751; CAN62488.1; -; Genomic_DNA.
DR   ExpressionAtlas; A5AHA8; baseline and differential.
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:SF132; HEAT SHOCK COGNATE PROTEIN 80-LIKE; 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   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}.
FT   DOMAIN          27..182
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          217..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..238
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   699 AA;  80012 MW;  0B98D76C489709C4 CRC64;
     MAETETFAFQ AEINQLLSLI INTFYSNKEI FLREIISNSS DALDKIRFES LTDKSKLDAQ
     PELFIHIVPD KTNNSLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
     FGVGFYSAYL VAEKVIVTTK HNDDEQYVWE SQAGGSFTVT RDTSGESLGR GTKITLYLKE
     DQLEYLEERR LKDLIKKHSE FISYPISLWI EKTTEKEISD DEDEEDKKDE EGKVEEVDEE
     KEKEEKKKKK IKEVSHEWSL VNKQKPIWMR KPEEITKEEY AAFYKSLTND WEEHLAVKHF
     SVEGQLEFKA ILFVPKRAPF DLFDTRKKPN NIKLYVRRVF IMDNCEELIP EYLGFVKGIV
     DSEDLPLNIS REMLQQNKIL KVIRKNLVKK CLELFFEIAE NKDDYNKFYE AFSKNLKLGI
     HEDSQNKGKL AELLRYHSTK SGDELTSLKD YVTRMKEGQN DIYYITGESK KAVENSPFLE
     KLKKKGIEVL FMVDAIDEYA VGQLKEFEGK KLVSATKEGL KLDESEDEKK KQEALKEKFE
     GLCKVIKDVL GDRVEKVVVS DRVVDSPCCL VTGEYGWTAN MERIMKAQAL RDSSMAGYMS
     SKKTMEINPE NPIMEELRKR ADADKNDKSV KDLVLLLFET ALLTSGFSLD EPNTFGNRIH
     RMMKLGLSID EDGPEADXXM PPLEEADADA EGSKMEEVD
//
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