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Database: UniProt
Entry: W9J1P2_FUSOX
LinkDB: W9J1P2_FUSOX
Original site: W9J1P2_FUSOX 
ID   W9J1P2_FUSOX            Unreviewed;       784 AA.
AC   W9J1P2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   22-FEB-2023, entry version 34.
DE   SubName: Full=Heat shock 70kDa protein 4 {ECO:0000313|EMBL:EWZ00893.1};
GN   ORFNames=FOYG_00624 {ECO:0000313|EMBL:EWZ00893.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWZ00893.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWZ00893.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; JH717839; EWZ00893.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9J1P2; -.
DR   OrthoDB; 276440at2759; -.
DR   Proteomes; UP000030753; 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; 1.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW   Stress response {ECO:0000313|EMBL:EWZ00893.1}.
FT   REGION          502..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  86740 MW;  3341416F7C09B2EC CRC64;
     MSVVGIDFGT LKTVIAVARN RGVDVVTNEV SNRATPSLVG FGPKSRYLGE AAKTQEISNL
     KNTVSSLKRL AGRQFNDPDI QIEQQYVTAP LADCNGQVGA EVNYLGKKEK FTATQLVAMY
     LSKIKQTAGA ELKLPVQDVC LSVPPWFTDV QRRALIDAAE IAGLRVLRLI NDGTAAALGW
     GITKLDLPAP EEAPRRVCFV DIGHSSYTVS IVEFKKGELA VKATTWDKDF GGRDFDRALV
     DHLAKEFKGK YKVDIMTHGR ALARTIAAAE KTKKILSANQ QAPVNIESLM NDIDASAMIT
     RQEFEAMIEP LLARTHLPLE EALAQAKLTK DDIDVIEVVG GGSRVPALKE RIQEFFGKPL
     SFTLNADEAL ARGSAFSCAI LSPVFRVRDF SVQDIISYPI EFAWEKAPDI PDEDTSLTVF
     NKGNVMPSTK ILTFYRKQPF DLEARYAQPE LLPGKTNPWI GRFSVKNVKA DGKDDFMICK
     LKARVNIHGV LNVETGYYVE EEEVEEEVNE DPDVSLSEPY MASNDFPPVH DQDSASSSSA
     SVGDDSRAYP AKRPRLDDEE ETDSSRSAFA VPEHLEESIY EPRSLTSVSQ KAMETDKDAP
     KKTRKVKKQV RKGDLPISTG SASLDDSTKA SLLEKEAAMV MEDKLVADTE EKKNELEAYI
     YDLRAKLDEQ YSEFASEEEK QTIKAKLEAT EDWLYEEGDD TTKGVYVAKI DEIRAMAGPI
     VQRHFEKVEA ERQAALEKAE AERAAKKAEE DARKAAEAEK ANTDQEMKDA DAPQQETEGS
     ADPQ
//
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