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}.
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; 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
//