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Database: UniProt
Entry: A0A024T8W3_9STRA
LinkDB: A0A024T8W3_9STRA
Original site: A0A024T8W3_9STRA 
ID   A0A024T8W3_9STRA        Unreviewed;       787 AA.
AC   A0A024T8W3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Chaperone DnaK {ECO:0000313|EMBL:ETV90458.1};
GN   ORFNames=H310_14759 {ECO:0000313|EMBL:ETV90458.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV90458.1};
RN   [1] {ECO:0000313|EMBL:ETV90458.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV90458.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; KI914036; ETV90458.1; -; Genomic_DNA.
DR   RefSeq; XP_008880907.1; XM_008882685.1.
DR   AlphaFoldDB; A0A024T8W3; -.
DR   STRING; 157072.A0A024T8W3; -.
DR   EnsemblFungi; H310_14759-t26_1; H310_14759-t26_1-p1; H310_14759.
DR   EnsemblProtists; ETV90458; ETV90458; H310_14759.
DR   GeneID; 20091809; -.
DR   VEuPathDB; FungiDB:H310_14759; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   eggNOG; KOG0548; Eukaryota.
DR   OrthoDB; 50968at2759; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF502; SHOCK COGNATE 70 KDA PROTEIN 2, PUTATIVE, EXPRESSED-RELATED; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SMART; SM00028; TPR; 3.
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   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
DR   PROSITE; PS50005; TPR; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   REPEAT          29..62
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          97..130
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   COILED          130..185
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   787 AA;  86688 MW;  A4DE6C8688A3471A CRC64;
     MAPPRRRANK KAGSDAYANL SADERKVQGA EAKTRGNTAY SAGDFNLAIK EFTTAIAYEP
     HNNAYYSNRS AAYLNNGNAA AALQDANKCI EIDPKWAKGY ARLGAAYFFV KSYEKAITAY
     TKGLSLDKGN KQLQAGLTQA QAALQVLEEE LSGVEMDDAT RKLKRLEIEE KINKARAERE
     ERAKRAERGF SEVIGIDLGT TYSCVGVWKD GQVEIIANSE GNRTTPSWVA FNETERLIGE
     AAKIQAASNA TNTVFDAKRI IGRNFSDPIV KKDAAHFPFK ISKGEGDKPL IQVTFRGEDK
     SFTPEEISSM VLTRMKETAE NFLGQEIKQA VVTVPAYFND QQRQSTKDAG AIAGLDVKRI
     INEPTAAALA YGLDTNAGAE GKSNILIFDL GGGTFDVSIL SIENGIFEVK ATGGDTHLGG
     EDFDSNMVDF LVTEFKRKNR NLDPTSSARS MRRLRTACES AKRMLSTTTS ATIEVDALFE
     GVDFSSTMTR AKFESLNEEC FKRTEETVLK VLQDANMKPD QISELVLVGG STRIPKVQTM
     LSNLFGGKEL SKSINPDEAV AYGAAVQGAI LSGIRNDATN SLLLVDVTPL SLGIELVGKV
     MSVLIKRNTA IPVKKTRIYT TEEDFQTSEK VVIYEGERAS VVDNNKLGEF EITGIERAKR
     GEPKLEVTFE IDANGILHVS CKDKKTGAKN QTTISNNRGR LSQEDIDRMV DEAEKYKKAD
     ALLLKRIEAR NDLEGFIYRY LEVASKKGEA QAENALRDAR DWLDEHAEAT VKELEDKKRA
     LERVCRF
//
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