ID A0A061FWX1_THECC Unreviewed; 417 AA.
AC A0A061FWX1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=DNAJ {ECO:0000313|EMBL:EOY19294.1};
GN ORFNames=TCM_044345 {ECO:0000313|EMBL:EOY19294.1};
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:EOY19294.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY19294.1, 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).
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DR EMBL; CM001888; EOY19294.1; -; Genomic_DNA.
DR RefSeq; XP_007010484.1; XM_007010422.2.
DR AlphaFoldDB; A0A061FWX1; -.
DR SMR; A0A061FWX1; -.
DR STRING; 3641.A0A061FWX1; -.
DR EnsemblPlants; EOY19294; EOY19294; TCM_044345.
DR EnsemblPlants; Tc10v2_t009820.1; Tc10v2_p009820.1; Tc10v2_g009820.
DR GeneID; 18586851; -.
DR Gramene; EOY19294; EOY19294; TCM_044345.
DR Gramene; Tc10v2_t009820.1; Tc10v2_p009820.1; Tc10v2_g009820.
DR KEGG; tcc:18586851; -.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; A0A061FWX1; -.
DR OMA; QHYNGEA; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000026915; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888:SF10; DNAJ-LIKE-2, ISOFORM A; 1.
DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 13..74
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 135..219
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 135..219
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 390..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 46577 MW; 6137E79789DD2851 CRC64;
MFGRAPKKSD NTKYYEILGV SKNASQDDLK KAYRKAAIKN HPDKGGDPEK FKELAQAYEV
LSDPEKREIY DQYGEDALKE GMGGGGGGHD PFDIFQSFFG GNPFGGGGSS RGRRQRRGED
VIHPLKVSLE DLYNGTSKKL SLSRNIICFK CKGKGSKSGA SMKCSGCQGS GMKVSIRHLG
PSMIQQMQHP CNECKGTGET INDKDRCPQC KGEKVVQEKK VLEVIVEKGM QNGQRITFPG
EADEAPDTVT GDIVFVLQQK EHPKFKRKGD DLFVEHTLTL TEALCGFQFI LTHLDGRQLL
IKSQPGEVVK PDQFKAINDE GMPMYQRPFM RGKLYIHFTV DFPDSLIPDQ CKALEAVLPP
RTSVQLTDME LDECEETTLH DVNIEEEMRR KQAQAQEAYE EDEDMHGGAQ RVQCAQQ
//
