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Database: UniProt
Entry: A0A2I1HB71_9GLOM
LinkDB: A0A2I1HB71_9GLOM
Original site: A0A2I1HB71_9GLOM 
ID   A0A2I1HB71_9GLOM        Unreviewed;       528 AA.
AC   A0A2I1HB71;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=70 kDa heat shock protein 1 {ECO:0000313|EMBL:PKY56090.1};
GN   ORFNames=RhiirA4_476117 {ECO:0000313|EMBL:PKY56090.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY56090.1, ECO:0000313|Proteomes:UP000234323};
RN   [1] {ECO:0000313|EMBL:PKY56090.1, ECO:0000313|Proteomes:UP000234323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY56090.1,
RC   ECO:0000313|Proteomes:UP000234323};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2015) 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:PKY56090.1}.
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DR   EMBL; LLXI01002059; PKY56090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1HB71; -.
DR   VEuPathDB; FungiDB:FUN_020900; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1880254; -.
DR   VEuPathDB; FungiDB:RhiirA1_466742; -.
DR   OrthoDB; 1384731at2759; -.
DR   Proteomes; UP000234323; 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   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; 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; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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:UP000234323};
KW   Stress response {ECO:0000313|EMBL:PKY56090.1}.
SQ   SEQUENCE   528 AA;  59086 MW;  913BEC146DCB24D6 CRC64;
     MATVGIDLGN AYTLVGVWIN DDVEIIVNKW GNRMTPSYVA FTDTGILIGD PAKNQICRNP
     YNTVFDIYRL IGCNYNDSNI QLNLKHWPFR VIEKNGKPYV CIKYKGEEKD FAPEEILSMI
     LVEMKETAET FLGTQVKNIV ITVPSCFNYS QRQAVKVAGL IAGLNVIRIV GGSTAASIAY
     GLNMITTREE YIVLIIDLGG GTCTVSLLTI EYGIYQVKAV AGNGHLGGED FDNRLINHFL
     QEFKSKFKKD LSSDARALCR LREHCERAKC TLSTSTHSFI EIDYLFEDID FYTSLTRTKF
     EELNQDLFQP IMELIEKVLE DSRFDKSHVH EIVLVGGSTC IPKIQRMISE FFNGKELNKS
     INPNEAAVYG AAVQAAVLSG NLSEKLLDFL LLDATALSLG IETLGGTFMP FVKRNTIIPN
     KKSEIISTDF DDQPNILIRV YEGERTQTRD NNFLGKVELS GIPPAPKDVP QIEVTFDVDQ
     NGILIVSAVD KSTGRSSKIT IEGRLLKEEI EHMVTETKKY HAERCKVL
//
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