ID A0A061E037_THECC Unreviewed; 551 AA.
AC A0A061E037;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE SubName: Full=Mitochondrial HSO70 2 isoform 1 {ECO:0000313|EMBL:EOX98330.1};
GN ORFNames=TCM_007119 {ECO:0000313|EMBL:EOX98330.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX98330.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX98330.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CM001880; EOX98330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061E037; -.
DR EnsemblPlants; EOX98330; EOX98330; TCM_007119.
DR Gramene; EOX98330; EOX98330; TCM_007119.
DR Proteomes; UP000026915; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 1.20.1270.10; -; 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; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT REGION 516..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 296..323
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 551 AA; 59121 MW; CAB7F176A3256F81 CRC64;
MATAALLRSF RRRDVASAPL SAYRCLTSNG KTSGGINWAS FSRAFSSKPA GNDVIGIDLG
TTNSCVAVME GKNPKVIENS EGARTTPSVV AFNQKGELLV GTPAKRQAVT NPTNTVFGTK
RLIGRRYDDP QTQKEMGMVP YKIVKAPNGD AWVEANGQQY SPSQIGAFIL TKMKETAESY
LGKGVSKAVI TVPAYFNDAQ RQATKDAGRI AGLDVQRIIN EPTAAALSYG MNNKEGLIAV
FDLGGGTFDI SILEISNGVF EVKATNGDTF LGGEDFDNAL LDFLVSEFKK TEGIDLSKDR
LALQRLREAA EKAKIELSST SQTEINLPFI TADASGAKHL NITLTRSKFE SLVNHLIERT
KTPCKNCLKD AGISTKDVDV PPAPRGMPQI EVTFDIDANG IVTVSAKDKA TGKEQQITIR
SSGGLSEDEI EKMVKEAELH AQKDQQRKAL IDIKNNADTT IYSVEKSLNE YRDKIPSEIA
KEIEDAVSDL RKAMEGENVD EIKAKIDAAN KAVSKIGEHM SGGSGGAQGG SAGGAQGGDQ
APEAEYEEVK K
//
