ID A0A059AJT0_EUCGR Unreviewed; 652 AA.
AC A0A059AJT0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW53916.1};
GN ORFNames=EUGRSUZ_J03127 {ECO:0000313|EMBL:KCW53916.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW53916.1};
RN [1] {ECO:0000313|EMBL:KCW53916.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW53916.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; KK198762; KCW53916.1; -; Genomic_DNA.
DR RefSeq; XP_010034044.1; XM_010035742.2.
DR AlphaFoldDB; A0A059AJT0; -.
DR STRING; 71139.A0A059AJT0; -.
DR EnsemblPlants; KCW53916; KCW53916; EUGRSUZ_J03127.
DR Gramene; KCW53916; KCW53916; EUGRSUZ_J03127.
DR eggNOG; KOG0101; Eukaryota.
DR InParanoid; A0A059AJT0; -.
DR OMA; GANDGMP; -.
DR OrthoDB; 3028330at2759; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375:SF495; HEAT SHOCK 70 KDA PROTEIN; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322}.
FT REGION 616..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 71470 MW; 3DE13F2A14F5901B CRC64;
MASKAIGIDL GTTYSCVAVW QNDRVEIIAN DQGNRTTPSY VAFTDTERLI GDAAKNQVAM
NPHNTVFDAK RLIGRRFSDP SVQADMKHWP FRVVSGPGDK PMIVVTFKGE EKQFSPEEIS
SMVLTKMKEI AEAFLGHPIK NAVITVPAYF NDSQRQATKD AGAIAGMNVL RIINEPTAAA
IAYGLDKKAA RAGEKNVLIF DLGGGTFDVS LLTIEEGIFE VKATAGDTHL GGEDFDNRLV
NHFVQEFKRK HKKDISGNAR ALRRLRTACE RAKRTLSSTS QTTIEIDSLY EGIDFYATIT
RARFEELNMD LFRRCMEPVE KCLRDAKIDK SQVHDVVLVG GSTRIPKVQQ LLQDFFNGKE
LCKSINPDEA VAYGAAVQAA ILSGEGNERV QDLLLLDVTP LSLGIETAGG VMTVLIPRNT
TIPTKKEQVF STYSDNQTSV LIQVYEGERA RTKDNNLLGT FELKGIPPAP RGVPQINVCF
DIDANGILNV SAEDKTAGVK NQITITNDKG RLSKEDIERM VQEAEKYKAE DEGVKKKVEA
KNALENYAYN MRNTVRDDKF AGKLDPADKQ KIEKAIDEAI EWLDRNQLAE VDELEDKLKE
LEGLCNPIIA KMYQGGPGGG DVPMGDMPGG GYGKPKSGGS GGGAGPKIEE VD
//
