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Database: UniProt
Entry: A0A372RD89_9GLOM
LinkDB: A0A372RD89_9GLOM
Original site: A0A372RD89_9GLOM 
ID   A0A372RD89_9GLOM        Unreviewed;       838 AA.
AC   A0A372RD89;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   SubName: Full=Heat shock protein 70 family {ECO:0000313|EMBL:RGB37820.1};
GN   ORFNames=C1646_813062 {ECO:0000313|EMBL:RGB37820.1};
OS   Rhizophagus sp. MUCL 43196.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB37820.1, ECO:0000313|Proteomes:UP000263633};
RN   [1] {ECO:0000313|EMBL:RGB37820.1, ECO:0000313|Proteomes:UP000263633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB37820.1,
RC   ECO:0000313|Proteomes:UP000263633};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RGB37820.1}.
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DR   EMBL; QKKE01000112; RGB37820.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372RD89; -.
DR   STRING; 1803374.A0A372RD89; -.
DR   InParanoid; A0A372RD89; -.
DR   Proteomes; UP000263633; 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; cd10228; HSPA4_like_NDB; 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; PTHR45639:SF4; HSC70CB, ISOFORM G; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW   Stress response {ECO:0000313|EMBL:RGB37820.1}.
FT   REGION          504..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..797
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..838
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  94498 MW;  C660FE092C317EE4 CRC64;
     MSVVGIDFGN LSSKIAVARN RGIDVICNEV SNRATPSLVS FGPKKRYLGE AAKTQEISNF
     KNTVGSLKRL AGRTFQDKEI QEIEKEYINA ELVNEKGQLG VKVQYLGEDR VFTGTQLITM
     YFTKLREIAS VELKIPVSDV VISVPGWFTD VQRRSILDAA EISGLNCLRL MNDTTASALG
     YGITKTDLPE DKPRNVVFVD IGHSGYSVAV VSFIKGQLTI KSTAYDRHFG GRDFDQVLVN
     HFAEVFKEKY KIDIKSNSKA LFRLRTAVEK LKKVLSANSQ APINVESIMN DVDVSAIMSR
     QEFEELSEHL ISRVENPLIQ ALQESGLKME EIHSVEVIGG STRIPALKER ISKFFGKELN
     FTLNQDEAVA RGCALQCAVL SPVFKVREFS VQDVTHYPIK IKWENILEIP DEESELVVFP
     KNNSIPSTKI LTFHRKQPFD IEAHYAEPDK IPAGINSWIG RFSIKEVVPT DSGDLSIIKV
     KARLNVHGVL SVESAYVVEE VIKEEKEEPP KQEKQEKQEK QEEQPKSDEP VPMETDNKPE
     EQQTQPKPQS PVTKKVKKLV KKNDLPLVSG VGSLDKTIIA QLKEIEGQMI ATDKLVADTE
     TQKNALEEYV YDMRGKLDTT YQEFVNPADK DTFINLLNET ENWLYDEGED ATKSTYMEKL
     DGLKKYGNPI VERYREAEEL PRAEKSLRDN IQHFILSASS NDERFNHIPD EEKKSVVEKA
     TKTSEWLNEK LAAQANVPKY ETPVVFVREI LKERENLVHF ASPILSKPKP KPEPKPEETP
     APTTADKQNS DTPKSEGTTT EDSAKVENEE TKEKKDEKTD ENTNENATNK DQSEMDVD
//
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