SSB1_MAGO7
ID SSB1_MAGO7 Reviewed; 614 AA.
AC G4NAY4;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Heat shock protein SSB1 {ECO:0000303|PubMed:30776962};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11484};
DE AltName: Full=HSP70 chaperone SSB1 {ECO:0000303|PubMed:30776962};
GN Name=SSB1 {ECO:0000303|PubMed:30776962}; ORFNames=MGG_11513;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, INTERACTION WITH HAT1, AND DISRUPTION PHENOTYPE.
RX PubMed=30776962; DOI=10.1080/15548627.2019.1580104;
RA Yin Z., Chen C., Yang J., Feng W., Liu X., Zuo R., Wang J., Yang L.,
RA Zhong K., Gao C., Zhang H., Zheng X., Wang P., Zhang Z.;
RT "Histone acetyltransferase MoHat1 acetylates autophagy-related proteins
RT MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and
RT pathogenicity in Magnaporthe oryzae.";
RL Autophagy 15:1234-1257(2019).
CC -!- FUNCTION: Chaperone that interacts with the histone acetyltransferase
CC HAT1 and mediates its translocation from the nucleus to the cytoplasm
CC during germination and starvation conditions. Within the cytoplasm,
CC HAT1 regulates autophagy via acetylation of the autophagy-related
CC proteins ATG3 and ATG9. {ECO:0000269|PubMed:30776962}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P11484};
CC -!- SUBUNIT: Interacts with HAT1 in starvation conditions.
CC {ECO:0000269|PubMed:30776962}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:30776962}. Cytoplasm
CC {ECO:0000305|PubMed:30776962}.
CC -!- DISRUPTION PHENOTYPE: Impairs the translocation of HAT1 from the
CC nucleus to the cytoplasm upon starvation.
CC {ECO:0000269|PubMed:30776962}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; CM001235; EHA48746.1; -; Genomic_DNA.
DR RefSeq; XP_003718330.1; XM_003718282.1.
DR AlphaFoldDB; G4NAY4; -.
DR SMR; G4NAY4; -.
DR STRING; 318829.MGG_11513T0; -.
DR EnsemblFungi; MGG_11513T0; MGG_11513T0; MGG_11513.
DR GeneID; 5050670; -.
DR KEGG; mgr:MGG_11513; -.
DR VEuPathDB; FungiDB:MGG_11513; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR InParanoid; G4NAY4; -.
DR OMA; HQTTVQF; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000009058; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
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; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Germination; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Stress response;
KW Virulence.
FT CHAIN 1..614
FT /note="Heat shock protein SSB1"
FT /id="PRO_0000447268"
FT REGION 1..392
FT /note="Nucleotide binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 393..403
FT /note="Inter-domain linker"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 404..614
FT /note="Substrate binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT REGION 517..613
FT /note="Lid domain (SBDalpha)"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT MOTIF 575..583
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 16..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 206..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 272..279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G0SCU5"
SQ SEQUENCE 614 AA; 66666 MW; C549DBC17B9FC6D9 CRC64;
MSTEVYDGAI GIDLGTTYSC VATYEGSNVE IIANEQGSFT TPSFVSFTAD ERLIGEAAKN
QAAMNPANTV FDVKRLIGRR FDDPTVKKDM ESWPFKVVDE DGNPKVEVEY LGTTHKFSPQ
EISAMVLVKM KEIAEAKIGK KVEKAVITVP AYFNDNQRQS TKDAGAISGL NVLRIINEPT
AAAIAYGLGS GKSEKERNVL IYDLGGGTFD VSLLNIQGGV FTVKATAGDT HLGGQDFDTN
LLDHCKKDFQ RKTKKDLSGD ARALRRLRTA CERAKRTLSN GTQTTLEIDS LFDGEDFSLQ
ITRAKFEELN QTAFKGTLDP VTQVLKDAGV DKAAVDEIVL VGGSTRIPKI QKLLSDYFGG
KKLEKSINPD EAVAYGAAVQ AGILSGKATS AETADLLLLD VVPLSLGVAM EGNIFAPVVP
RGTTVPTLKK RSFTTVADQQ QTVQFPVYQG ERTNCSENVS LGEFTLAPIP PMRAGEPVLE
VVFEVDVNGI LKVTATEKTS GRSANITIAN SVGKLSTSEI ENMISEAEKY KTNDEEFTKK
HEAKQQLESY IARVEDIISD PTLALKLKRG QKEKIENTMS EAMAQLELGE STADDLKKKE
LALKRAVTKA MSSR
