ID A0A0E0H3W5_ORYNI Unreviewed; 752 AA.
AC A0A0E0H3W5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=DnaJ homolog subfamily C member 2 {ECO:0000256|ARBA:ARBA00014469};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA04G19030.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA04G19030.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA04G19030.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA04G19030.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA04G19030.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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 AlphaFoldDB; A0A0E0H3W5; -.
DR STRING; 4536.A0A0E0H3W5; -.
DR EnsemblPlants; ONIVA04G19030.1; ONIVA04G19030.1; ONIVA04G19030.
DR Gramene; ONIVA04G19030.1; ONIVA04G19030.1; ONIVA04G19030.
DR eggNOG; KOG0048; Eukaryota.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_370236_0_0_1; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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 CDD; cd00167; SANT; 2.
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; 1.10.10.60; Homeodomain-like; 2.
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; IPR009057; Homeobox-like_sf.
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 InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR43888:SF36; CHAPERONE PROTEIN DNAJ A6; 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 Pfam; PF00249; Myb_DNA-binding; 2.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
DR PROSITE; PS50090; MYB_LIKE; 2.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000006591};
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 26..78
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 26..74
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 79..134
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 87..130
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 348..409
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 469..553
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 469..553
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 83424 MW; B6AE323941525A21 CRC64;
MARAPGGVRR RSGRRGAGGG GAGGGGEALR KGPWMAEEDE VLLEHVRTHG PMDWSSIRSK
GLLPRTGKSC RLRWVNKLRP NLKSGCKFTA EEERVVIELQ AQFGNKWARI ATYLQGRTDN
DVKNFWSTRQ KRLARLLRGP LPAARPNKHN SGKGKAPSSS SLDSQTATFH QSSASLDQAS
LEGNSLGWQC REAAPFMGYD QACSGFFAFE GPLPLQLLPP ADGEASSSNA AQSAPPPLLF
DQPPYPLINF PGWPERYVDV GHGFVDAGAM DGLAYQELLP MVQSVPMIMP FFGMECAHDA
VKHGAFDDLP PNMFDDAVDQ PPPPPPPPPP PSPSPSPSRD DVLSNNTKYY EVLGVPKTAS
KDELKKAYRK AAIKNHPDKG GDPEKFKELS QAYEVLTDPE KRDIYDQYGE DALKDGMGGG
SDFHNPFDIF EQFFGGGAFG GSSSRVRRQR RGEDVVHTLK VSLEDVYNGS MKKLSLSRNI
LCPKCKGKGT KSEAPATCYG CHGVGMRNIM RQIGLGMIQH MQTVCPECRG SGEIISDRDK
CTNCRASKVI QEKKVLEVHI EKGMQHGQKI VFQGEADEAP DTVTGDIVFI LQVKVHPRFK
RKYDDLFIER TISLTEALCG FQFILTHLDS RQLLIKANPG EIIKPGQHKA INDEGMPHHG
RPFMKGRLFV EFNVEFPESG VLSRDQCRAL EMILPPKPGH QLSDMDLDQC EETTMHDVNI
EEEMRRKQYQ RKQEAYDEDE EEDAPRVQCA QQ
//
