ID   B2WKN9_PYRTR            Unreviewed;      1013 AA.
AC   B2WKN9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Chaperone protein dnaK {ECO:0000313|EMBL:EDU43599.1};
GN   ORFNames=PTRG_10549 {ECO:0000313|EMBL:EDU43599.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU43599.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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DR   EMBL; DS231628; EDU43599.1; -; Genomic_DNA.
DR   RefSeq; XP_001940880.1; XM_001940845.1.
DR   AlphaFoldDB; B2WKN9; -.
DR   STRING; 426418.B2WKN9; -.
DR   EnsemblFungi; EDU43599; EDU43599; PTRG_10549.
DR   GeneID; 6348855; -.
DR   eggNOG; KOG0104; Eukaryota.
DR   HOGENOM; CLU_005965_5_0_1; -.
DR   InParanoid; B2WKN9; -.
DR   OMA; SRTPMIQ; -.
DR   OrthoDB; 5491443at2759; -.
DR   Proteomes; UP000001471; 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; cd10230; HYOU1-like_NBD; 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; IPR029048; HSP70_C_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..1013
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002784887"
FT   REGION          598..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..822
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..936
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..967
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1013 AA;  110100 MW;  55EABEAD66F20902 CRC64;
     MAPPGRRRGQ LSPATILLGL VFLFSSTASA ASAVIGVDLG TEYIKAALVK PGIPLEIVLT
     KDSKRKETSA VAFKPAKSGP LPPGSYPERF YGSDAIALQA RFPGDVYPNL KHLLGVSSES
     EIVGTYKERY PALEVTGTQD RNTVSFQSGV FSKDKSYTVE ELLAMELKNV RENAKALAGK
     AYDIQDVVFT VPAFYTVEER RALQVAARLA GLKVLSVVSD GLAVGLNYAT GRTFPDVTKD
     GKPEINLVFD MGAGSTSASV VKFQGRTVKD VGKRNKTVQE VQVMGTGWDR TLGGDALNSL
     IVDDMVSTFT ELPAAKSASL TADKVKTHGR TAAKLFKEAE RVRQMLSANK ETNSFFESFH
     EDIDFRYKFS RTKFEELTAA YAARVDGPIN RALEAAGLTI ADIDSVIVHG GASRTPFVQA
     RLEAVAGKNK IRANVNADEA AVFGAAFKAA SLSPSFRVKE IRDSDIQGYN HGIQYSFNLK
     DRDQKIFTPT TKLGATKDLP FQMMGEFEFT IYQALPRANG DVSKEPTLRF SSGNLTRAVT
     KMIDEDKCDR QSFNNYVQVR LSPITGTPEI VSAWVTCETE EAKGGIVDGV KNLFGMGGKK
     DQEPLKEGES SSSSASASSS SSTSSSADAE STDAAKPDEK KIKTVKSAIT FDVEQLGYKK
     IPRKELKRMQ DRLAAFDSSD KSRRLREEGL NSLEAFTYRA RDYLEDESFI GASTAAVRES
     LEKALSAASE WIYSEGAEAD EKTLKSKLKE LEDIVNPILK RKNEAAKRPD AIKDFKDTIA
     HIKEVIQLVD NQIKTQSYES SKSSEAVSKA SAEASASPSS TEAIDELDEE VDAPAQPEIT
     EVSTVYTESD LTTVQEAASK AQAWIDENEA KQSKLGATDD PAFTVKDIAA EKKKLDDVIM
     DMMMKKMKHF KPPNQQKPKA SKPKSKSAKG KKNASKSKKA ATKETDAPAA GDGPSREELE
     EALKKAGVNK PNGDNNILNK LNLDKDASEE EILAAISKAT KEGRLKDEGH SEL
//