ID W5LWA8_LEPOC Unreviewed; 858 AA.
AC W5LWA8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Heat shock protein family H (Hsp110) member 1 {ECO:0000313|Ensembl:ENSLOCP00000000415.1};
GN Name=HSPH1 {ECO:0000313|Ensembl:ENSLOCP00000000415.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000000415.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000000415.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR RefSeq; XP_015194712.1; XM_015339226.1.
DR AlphaFoldDB; W5LWA8; -.
DR STRING; 7918.ENSLOCP00000000415; -.
DR Ensembl; ENSLOCT00000000415.1; ENSLOCP00000000415.1; ENSLOCG00000000380.1.
DR GeneID; 102691519; -.
DR KEGG; loc:102691519; -.
DR CTD; 10808; -.
DR eggNOG; KOG0103; Eukaryota.
DR GeneTree; ENSGT00940000159635; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; W5LWA8; -.
DR OMA; NEFTDRC; -.
DR OrthoDB; 276440at2759; -.
DR Proteomes; UP000018468; Unassembled WGS sequence.
DR Bgee; ENSLOCG00000000380; Expressed in brain and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
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:0006457; P:protein folding; IBA:GO_Central.
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:UP000018468}.
FT REGION 515..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 96641 MW; AE25253E0CBD0081 CRC64;
MSVVGFDVGF QNCYIAVARA GGIETVANEF TDRCTPAVVS FGSKNRTIGN AAKNHLITNA
RNTVFNFKRL HGRPFQDPVV QSEKANLPYD LVPLQNGSVG AKVMYLDEEH HFSVGQIMAM
LLTKMKETAE NNLQKKVTDC VISVPTFFTD AERRSVLDAS QIAGLNCLRL MNDTTAVALN
YGIYKQDLPS PEEKPKIVVF VDMGHSAFQV SACAFNKGKL KVLATAFDPY LGGRNFDQRL
VDYFSVEFKS KYNLDVKSRV RALLRLHQEC EKLKKLMSSN STDIPLNIEC FMDDKDVAGK
MNRAQFEEMC ADLIERVVAP LKAVVEQAQL QLQDISSVEI VGGATRIPAV KERIVKFFGK
DVSTTLNADE AVARGCALQC AILSPAFKVR DFSITDAVSF PVSLSWSTEV DEPMGNHEVF
CKNHISPFSK VITFYRRDPF MLEAFYTDPN TLPYPEAKIG QFTVQNVTPQ DDGEKSKVKV
KVRVNAHGIV SVSSASMVQK VKTEDDDSTS IMDDMEEEAN SQESTVIVDG ENKAPGKSEG
ETLPHIQIEN HQAQSPPSPD PTEEGKQNDV TPQKVNGELK AHQPPEAKKP KIKVKNVDLP
IQAELVWQLG KEQLNAYLEQ EGKMQIQDKL ENERNNAKNA VEEYVYYFRH KLEGPYEVFV
SKQDREKFTQ LLDQTENWLY DEGEDQPKQA YLDKMEELKK LGMPVQERYQ EAEVRPKLFE
EITSKMQAYV KITEDYRNGD EKYIHIDAPD MEKVTKCVRE TMEWVNNVKN AQDQLQPDQD
PVVRVAQIKA KLKELYITCE PVVSKPKPRV ESPVEDNGQI EENASIKKTE AKTMEEHVIT
PEEISQNGIN GTTNMDLN
//
