ID   M7CN28_CHEMY            Unreviewed;       742 AA.
AC   M7CN28;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Heat shock protein 105 kDa {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=UY3_00132 {ECO:0000313|EMBL:EMP42667.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP42667.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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; KB469743; EMP42667.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7CN28; -.
DR   STRING; 8469.M7CN28; -.
DR   eggNOG; KOG0103; Eukaryota.
DR   Proteomes; UP000031443; 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:UP000031443}.
FT   REGION          463..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMP42667.1"
SQ   SEQUENCE   742 AA;  83596 MW;  CE0E7B47894ED720 CRC64;
     ITHANNTVSN FKRFHGRAFN DPFIQKEKES LSYDLVPMKN GGVGIKVLYM GEEHFFSVEQ
     ITAMLLTKLK ETAETNLKKP VTDCVISVPS FFTDAERRSV LDAAQIVGLN CLRLMNDMTA
     VALNYGIYKQ DLPAPEEKPR IVVFVDMGHS AFQVSACAFN KGKLKVLGTA FDPFLGGRNF
     DEKLVDHFCV EIKAKYKLDP KSKIRALLRL YQECEKLKKL MSSNSTDIPL NIECFMNDRD
     VAGKMNRSQF EELCAELLQR IEGPLHSLME QTQFKVEDVN AVEIVGGATR IPAVKEKIAK
     FFGKDVSTTL NADEAVARGC ALQCAILSPA FKVREFSVTD AVPFPISLMW NTEADDTEGV
     HEVFSRNHAA PFSKVLTFYR KGPFELEAFY SDPNGVPYPE TKIGRYIVQN VAAQKDGERS
     KVKVKVRVNT HGIFSVSTAS MVEQVKAEEN EDLSVETEVV IVNQRPPENS DDKNIQQDNN
     EAGTQSQVQT DGQPTPQSPP SPEPSSEENK IPDAKKTNEK KSDQPPEAKK PKIKVKNVEL
     PIEANLDLQK FSAFLTEIED WLYEDGEDQA KQVYIDKLDD LKKLGTPIEM RYQEAEEQPR
     VLEELGHKLQ HYAKIAGEYR DKDEKYIHID ESEMIEVEKC VKEMMEWMSN VMNAQAKMSL
     DQDPVVRASE IKAKLKELHS VCEPIVLQPK PNVDSPKEEN PLNGPSLHTN EGMEEDKNNA
     EIHQQNGDCH PNDKNTTSMD LD
//