ID A0A0R0M3F3_9MICR Unreviewed; 710 AA.
AC A0A0R0M3F3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Molecular chaperones HSP70/HSC70, HSP70 superfamily {ECO:0000313|EMBL:KRH92907.1};
DE Flags: Fragment;
GN ORFNames=M153_213700093 {ECO:0000313|EMBL:KRH92907.1};
OS Pseudoloma neurophilia.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pseudoloma.
OX NCBI_TaxID=146866 {ECO:0000313|EMBL:KRH92907.1, ECO:0000313|Proteomes:UP000051530};
RN [1] {ECO:0000313|EMBL:KRH92907.1, ECO:0000313|Proteomes:UP000051530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:KRH92907.1,
RC ECO:0000313|Proteomes:UP000051530};
RA Ndikumana S., Pelin A., Sanders J., Corradi N.;
RT "The genome of Pseudoloma neurophilia, a relevant intracellular parasite of
RT the zebrafish.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {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:KRH92907.1}.
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DR EMBL; LGUB01000596; KRH92907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0M3F3; -.
DR VEuPathDB; MicrosporidiaDB:M153_213700093; -.
DR Proteomes; UP000051530; 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; cd10170; HSP70_NBD; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 4.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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:UP000051530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..710
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006399111"
FT REGION 329..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 710
FT /evidence="ECO:0000313|EMBL:KRH92907.1"
SQ SEQUENCE 710 AA; 80112 MW; 886302588252D79D CRC64;
MLKNLFLFTL LVVIYTLTDD QNKKGLKVCV GIDLGTTYSS VAIVPKSGVA DLDILDIGGG
RTTLPSVIRY DPIKLSAKDK ITWIPKTGWD VFLSNLKNPT PNSYIYAFKR YMGIASIEDE
PKLKGINEKV TYSIIEEKKG ENTSLYMEIK DINNKTVKKV SAIDASATIL ETLIEIVNEK
YGKENIENVI ITVPAYFSET QVKATKTAAT IANLTVQRTV NEPVAAAYAY QIRYAQEPVD
SYLVFDFGGG TLDISILEYE SGVLEVVTYS GSNFLGGENI NDCLFKYFYS ILKNKNILLD
DVEMLRLRGF TEKFKISLCN KILLSENNKG GKGNDNNNKR SNNIDNNLND KINLDNNNKR
NNKDNNDKDN KDNNNNNNNN KDNNNLNNNN NNNDVIEFSD DFIYLGNKVE NFTLSDKKFK
SICKPIIDEI IDQLTGPTGV LTKYKNKWEK DKSDIQKVLL VGGSTRVPFV REILSQLFTK
EKVSSELNPD TVVAEGAALY AANMLDWLKD DSLHLIDVVP MNIGICVDTD TFESILDMES
AIPASQVKTF TTGQDNQSMV KIKVAQGVRY QYHKNQHLGQ FELTLKDPKP KGIPQIEVSV
SINKEREIFV KATDKATGLE EKIQFVKKDY ELSDQRRQEM LKDRDSNKSL DESLKKKDSN
IKELETYKDS INHSIIQLGE KINESERTLL FKEISKVEEF LKDAKNPMAG
//