ID   A0A091EJY8_CORBR        Unreviewed;       803 AA.
AC   A0A091EJY8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 26.
DE   SubName: Full=Heat shock protein 105 kDa {ECO:0000313|EMBL:KFO57391.1};
DE   Flags: Fragment;
GN   ORFNames=N302_00892 {ECO:0000313|EMBL:KFO57391.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO57391.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO57391.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO57391.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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; KK718531; KFO57391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091EJY8; -.
DR   STRING; 85066.A0A091EJY8; -.
DR   Proteomes; UP000052976; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 2.
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; PTHR45639:SF2; HEAT SHOCK PROTEIN 105 KDA; 1.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 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; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW   Stress response {ECO:0000313|EMBL:KFO57391.1}.
FT   REGION          448..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..535
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..784
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO57391.1"
FT   NON_TER         803
FT                   /evidence="ECO:0000313|EMBL:KFO57391.1"
SQ   SEQUENCE   803 AA;  90763 MW;  1D6DB9FF178E0376 CRC64;
     QQITHAHNTV SNFKRFHGRA FNDPFVQKEK EKLSYDLVPM KNGGVGVKVM YMDEEHIFSV
     EQISAMLLTK LKETAESNLK KPVTDCVISV PSFFTDAERR SLLDAAQIVG LNCLRLMNDM
     TAVALNYGIY KQDLPAPEEK PRIVVFVDMG HSAFQVSACA FNKSKLKVVL GTAFDPFLGG
     RSFDGKLVDY FCAEIKSKYK LDPKTKVRAL LRLYQECEKL KKLMSSNSTD IPLNIECFMN
     DTDVSGKMNR SQFEELCADL LQRIEMPLLS LMEQTQLKVE DVNAVEIVGG ATRIPGVRER
     IAKFFGKDVS TTLNADEAIA RGCALQCAIL SPAFKVREFS VTDATPFPIS LLWNTEAEDT
     EGVHEVFSRN HAAPFSKVLT FYRKGPFELE AFYSDPNGVP YPESKIGRYV IQNVAAQKDG
     EKSKVKVKVR VNTHGIFSVS TASMVEPVKS EECEDVSVET EVESQDQRPI ENLSDKNIQQ
     ENSEAGTQSQ VQTDGQQTSQ SPPSSEPPSE ENKIPDVKKT NEKKGDQPPE AKKPKIKVKN
     VELPIEANLV WQLGKDLLNM YIETEGKMIM QDKLEKERND AKNAVEEYVY EFRDKLSGPY
     EKFVCEKDLQ GFSALLAETE GWLYEEGEDE AKQVYVEKLE DLKKLGTPIE MRYQEAEERP
     RLLQELGHRL QYYATIAGEF RNKDEKYIHI DEMEMMKVEK CVSEVVEWMN NAVSAQAKKS
     LDQDPAVHSS EIKAKLQELN NVCEPVVTQP KPKVDSPKEE NPLSEQSDYK TEDMGEDDKN
     SEMPQQNGEC HPSDQNTINM DPD
//