ID A0A1Y2E555_9FUNG Unreviewed; 654 AA.
AC A0A1Y2E555;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=70 kDa heat shock protein 3 {ECO:0000313|EMBL:ORY66669.1};
GN ORFNames=LY90DRAFT_661073 {ECO:0000313|EMBL:ORY66669.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY66669.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY66669.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY66669.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY66669.1}.
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DR EMBL; MCOG01000050; ORY66669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2E555; -.
DR STRING; 1754190.A0A1Y2E555; -.
DR OrthoDB; 1327454at2759; -.
DR Proteomes; UP000193920; 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 CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
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; PTHR19375:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW Stress response {ECO:0000313|EMBL:ORY66669.1}.
FT REGION 614..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 71504 MW; A5D43A03020D43D2 CRC64;
MTKVSSIGID LGTTYSCVGV WQNDRVEIIP NDQGNRTTPS FVAFTDSERL IGDAAKNQAA
MNPTNTVFDA KRLIGRRFND SEVQSDMKHW PFKVVEKSGK PYIQVQFKGE TKDFTAEEIS
SMVLTKMKDT AEAYLGDKVS NAVITVPAYF NDSQRQATKD AGLIAGLNVL RIINEPTAAA
IAYGLDKKSE GEKNVLIFDL GGGTFDVSLL TIEDGIFEVK ATAGDTHLGG EDFDNRLVSH
FEQEFKRKYK KDISSNPRSL RRLRTACERA KRTLSSSTQT SIEIDSLYEG IDFYTSITRA
RFEELNSDLF RSVIEPVEKV LNDAKLDKSS IHEIVLVGGS TRIPKIQSLV SQYFNGKEPS
KSINPDEAVA YGAAVQAAIL SGETSEKTQD LLLLDVSPLS LGIETAGGVM TTLIKRNTTI
PTKKSDIFST YADNQTGVTI QIYEGERSLT KDNNLLGKFE LMGIPPAPRG VPQIEVTFDI
DANGILNVSA LDKTTGKSNK ITITNDKGRL SKEEIDRMVN DAEKYKEEDA KVAERVAAKN
GLESYAYQLR NTTQDEKIAK HIDGSDKEKL NKAIDETISW LDRNQEANKE EYESKRKELE
SIANPIMTKM YQQAGGAGAG AAPGGFPGSA PGGFPGSNGN NGGSNNGPTV EEVD
//