ID A0A0C7MX42_9SACH Unreviewed; 647 AA.
AC A0A0C7MX42;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE SubName: Full=LALA0S12e01420g1_1 {ECO:0000313|EMBL:CEP64548.1};
GN ORFNames=LALA0_S12e01420g {ECO:0000313|EMBL:CEP64548.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64548.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP64548.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64548.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; LN736371; CEP64548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7MX42; -.
DR STRING; 1245769.A0A0C7MX42; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000054304; 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 GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 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; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000054304}.
FT REGION 627..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 564..591
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 647 AA; 70110 MW; 0A509987797EFF06 CRC64;
MLSAKSIFRN SANPVRQFAR MNSNKVQGQV IGIDLGTTNS AVAIMEGKVP KIIENAEGAR
TTPSVVAFTK DGERLVGIPA KRQAVVNPEN TLFATKRLIG RRFEDIEVQR DIKQVPYKIV
KHTNGDAWLE ARGETYSPSQ IGGFVLNKMK ETAEAYLGKN VKNAVVTVPA YFNDSQRQAT
KDAGQIVGLN VLRVVNEPTA AALAYGLEKS DTKVVAVFDL GGGTFDISIL DIDNGVFEVK
STNGDTHLGG EDFDILLLRE IVQNFKKESG INLENDRMAI QRIREAAEKA KIELSSTVAT
EVNLPFITAD ASGPKHINMK FTRAQFESLT EPLIKRTVDP VKKALKDATL STSDVSDVIL
VGGMSRMPKV VETVKSLFNK EPSKAVNPDE AVAIGAAIQG AVLAGEVTDV LLLDVTPLSL
GIETLGGVFT RLIPRNTTIP TKKSQIFSTA AAGQTSVEIR VFQGERELVR DNKLIGNFTL
SGIPPAPKGV PQIEVSFDLD ADGIINVSAR DKASNKDASI TVAGSSGLSE SEIEQMVSDA
EKYREQDETR KKAIETSNKA DQLANDTESS LKEFEAKVDK AEAQKVKDQI TALREVVARV
QAGEEVDAED LKTKTEELQT ASMKLFEQMY KNDASSNSNP EGGEPKQ
//
